https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Christina+Chisholm 2026-09-30T00:37:05Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1878777 2013-12-20T22:40:24Z

<p>Christina Chisholm: </p> <hr /> <div>OmpG is a member of [[CBI Molecules]] being studied in the [http://www.chem.umass.edu/~chenlab/ Chen Lab] in the &lt;span class=&quot;plainlinks&quot;&gt;[http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program]&lt;/span&gt; at UMass Amherst and on display at the &lt;span class=&quot;plainlinks&quot;&gt;[http://www.molecularplayground.org/ Molecular Playground]&lt;/span&gt;.<br /> <br /> <br /> &lt;Structure load='2GTG' size='500' frame='true' align='right' caption='Outer Membrane Protein G' scene='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/5'&gt;<br /> <br /> <br /> ===Outer Membrane Protein G===<br /> Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection. The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, we utilize the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present. We propose the use of monomeric protein Outer membrane protein G (OmpG) will allow us to tailor and fine tune properties of this pore in detection of analytes. <br /> <br /> This &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/4'&gt;monomeric porin&lt;/scene&gt; has features that can be customized as a sensor component, using protein engineering we can develop this protein to be a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;Location of ligand&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> <br /> <br /> ==Structural Features of OmpG==<br /> OmpG is a 14-stranded beta-barrel and in contrast to most porins, appears to function as a monomer.[1] The central pore of OmpG is wider than other E. coli porins and it is speculated that it may form a non-specific channel for the passive transport of larger oligosaccharides.[1] OmpG adopts two conformations: open and closed. At neutral pH the porin displays an open conformation. However at a more acidic pH the closed conformation is adopted. This closed conformation is a result of OmpG's flexible extracellular loop 6, which folds across the channel blocking the pore opening. The rearrangement of loop 6 appears to be triggered by a pair of histidine residues, which repel one another at acidic pH, resulting in the breakage of neighbouring H-bonds and a lengthening of loop 6 from 10 to 17 residues[2,3]. &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> <br /> [[Image:OmpG Conformation.png | thumb| ]]<br /> [2IWW]<br /> [http://en.wikipedia.org/wiki/Outer_membrane_protein_G].<br /> <br /> ==Additional Resources==<br /> Current applications using nanopores for protein detection [https://www.nanoporetech.com/technology/analytes-and-applications-dna-rna-proteins/protein-analysis-]<br /> For additional information, see: Nanobiotechnology Review [http://www.nature.com/nnano/journal/v6/n4/full/nnano.2011.52.html]<br /> &lt;br /&gt;<br /> <br /> ==References==<br /> <br /> [1] Chen M, Li Q-H and Bayley, H (2008) &quot;Orientation of the monomeric porin OmpG in planar lipid bilayers.&quot; ChemBioChem 9(18):3029-36<br /> <br /> [2] Chen M, Khalid S, Sansom M and Bayley H (2008) &quot;Outer membrane protein G: engineering a quiet pore for biosensing.&quot; Proc Natl Acad Sci U S A 105: 6272-6277 <br /> <br /> [3] Damaghi M, Bippes C, et al. (2010) &quot;pH-dependent interactions guide the folding and gate the transmembrane pore of the beta-barrel membrane protein OmpG.&quot; J Mol Biol 397(4):878-82.</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1878776 2013-12-20T22:37:13Z

<p>Christina Chisholm: </p> <hr /> <div>OmpG is a member of [[CBI Molecules]] being studied in the [http://www.chem.umass.edu/~chenlab/ Chen Lab] in the &lt;span class=&quot;plainlinks&quot;&gt;[http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program]&lt;/span&gt; at UMass Amherst and on display at the &lt;span class=&quot;plainlinks&quot;&gt;[http://www.molecularplayground.org/ Molecular Playground]&lt;/span&gt;.<br /> <br /> <br /> &lt;Structure load='2GTG' size='500' frame='true' align='right' caption='Outer Membrane Protein G' scene='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/5'&gt;<br /> <br /> <br /> ===Outer Membrane Protein G===<br /> Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection. The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, we utilize the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present. We propose the use of monomeric protein Outer membrane protein G (OmpG) will allow us to tailor and fine tune properties of this pore in detection of analytes. <br /> <br /> This &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/4'&gt;monomeric porin&lt;/scene&gt; has features that can be customized as a sensor component, using protein engineering we can develop this protein to be a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;Location of ligand&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> <br /> <br /> ==Structural Features of OmpG==<br /> OmpG is a 14-stranded beta-barrel and in contrast to most porins, appears to function as a monomer.[1] The central pore of OmpG is wider than other E. coli porins and it is speculated that it may form a non-specific channel for the passive transport of larger oligosaccharides.[1] OmpG adopts two conformations: open and closed. At neutral pH the porin displays an open conformation. However at a more acidic pH the closed conformation is adopted. This closed conformation is a result of OmpG's flexible extracellular loop 6, which folds across the channel blocking the pore opening. The rearrangement of loop 6 appears to be triggered by a pair of histidine residues, which repel one another at acidic pH, resulting in the breakage of neighbouring H-bonds and a lengthening of loop 6 from 10 to 17 residues[2,3]. &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> [2IWW]<br /> [http://en.wikipedia.org/wiki/Outer_membrane_protein_G].<br /> <br /> ==Additional Resources==<br /> Current applications using nanopores for protein detection [https://www.nanoporetech.com/technology/analytes-and-applications-dna-rna-proteins/protein-analysis-]<br /> For additional information, see: Nanobiotechnology Review [http://www.nature.com/nnano/journal/v6/n4/full/nnano.2011.52.html]<br /> &lt;br /&gt;<br /> <br /> ==References==<br /> <br /> [1] Chen M, Li Q-H and Bayley, H (2008) &quot;Orientation of the monomeric porin OmpG in planar lipid bilayers.&quot; ChemBioChem 9(18):3029-36<br /> <br /> [2] Chen M, Khalid S, Sansom M and Bayley H (2008) &quot;Outer membrane protein G: engineering a quiet pore for biosensing.&quot; Proc Natl Acad Sci U S A 105: 6272-6277 <br /> <br /> [3] Damaghi M, Bippes C, et al. (2010) &quot;pH-dependent interactions guide the folding and gate the transmembrane pore of the beta-barrel membrane protein OmpG.&quot; J Mol Biol 397(4):878-82.</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1878764 2013-12-20T21:38:48Z

<p>Christina Chisholm: </p> <hr /> <div>OmpG is a member of [[CBI Molecules]] being studied in the [http://www.chem.umass.edu/~chenlab/ Chen Lab] in the &lt;span class=&quot;plainlinks&quot;&gt;[http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program]&lt;/span&gt; at UMass Amherst and on display at the &lt;span class=&quot;plainlinks&quot;&gt;[http://www.molecularplayground.org/ Molecular Playground]&lt;/span&gt;.<br /> <br /> <br /> &lt;Structure load='2GTG' size='500' frame='true' align='right' caption='Outer Membrane Protein G' scene='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/5'&gt;<br /> <br /> <br /> ===Outer Membrane Protein G===<br /> Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection. The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, we utilize the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present. We propose the use of monomeric protein Outer membrane protein G (OmpG) will allow us to tailor and fine tune properties of this pore in detection of analytes. <br /> <br /> This &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/4'&gt;monomeric porin&lt;/scene&gt; has features that can be customized as a sensor component, using protein engineering we can develop this protein to be a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;Location of ligand&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> <br /> <br /> ==Structural Features of OmpG==<br /> OmpG is a 14-stranded beta-barrel and in contrast to most porins, appears to function as a monomer.[1] The central pore of OmpG is wider than other E. coli porins and it is speculated that it may form a non-specific channel for the passive transport of larger oligosaccharides.[1] OmpG adopts two conformations: open and closed. At neutral pH the porin displays an open conformation. However at a more acidic pH the closed conformation is adopted. This closed conformation is a result of OmpG's flexible extracellular loop 6, which folds across the channel blocking the pore opening. The rearrangement of loop 6 appears to be triggered by a pair of histidine residues, which repel one another at acidic pH, resulting in the breakage of neighbouring H-bonds and a lengthening of loop 6 from 10 to 17 residues[2,3]. &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> [2IWW]<br /> [http://en.wikipedia.org/wiki/Outer_membrane_protein_G].<br /> <br /> ==Additional Resources==<br /> Current applications using nanopores for protein detection [https://www.nanoporetech.com/technology/analytes-and-applications-dna-rna-proteins/protein-analysis-]<br /> For additional information, see: Nanobiotechnology Review [http://www.nature.com/nnano/journal/v6/n4/full/nnano.2011.52.html]<br /> &lt;br /&gt;<br /> <br /> ==References==<br /> <br /> Chen M, Li Q-H and Bayley, H (2008) &quot;Orientation of the monomeric porin OmpG in planar lipid bilayers.&quot; ChemBioChem 9(18):3029-36<br /> <br /> Chen M, Khalid S, Sansom M and Bayley H (2008) &quot;Outer membrane protein G: engineering a quiet pore for biosensing.&quot; Proc Natl Acad Sci U S A 105: 6272-6277 <br /> <br /> Damaghi M, Bippes C, et al. (2010) &quot;pH-dependent interactions guide the folding and gate the transmembrane pore of the beta-barrel membrane protein OmpG.&quot; J Mol Biol 397(4):878-82.</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1878753 2013-12-20T15:31:02Z

<p>Christina Chisholm: </p> <hr /> <div>OmpG is a member of [[CBI Molecules]] being studied in the [http://www.chem.umass.edu/~chenlab/ Chen Lab] in the &lt;span class=&quot;plainlinks&quot;&gt;[http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program]&lt;/span&gt; at UMass Amherst and on display at the &lt;span class=&quot;plainlinks&quot;&gt;[http://www.molecularplayground.org/ Molecular Playground]&lt;/span&gt;.<br /> <br /> <br /> &lt;Structure load='2GTG' size='500' frame='true' align='right' caption='Outer Membrane Protein G' scene='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/5'&gt;<br /> <br /> <br /> ===Outer Membrane Protein G===<br /> Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection. The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, we utilize the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present. We propose the use of monomeric protein Outer membrane protein G (OmpG) will allow us to tailor and fine tune properties of this pore in detection of analytes. <br /> <br /> This &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/4'&gt;monomeric porin&lt;/scene&gt; has features that can be customized as a sensor component, using protein engineering we can develop this protein to be a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;Location of ligand&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> <br /> <br /> ==Structural Features of OmpG==<br /> OmpG is a 14-stranded beta-barrel and in contrast to most porins, appears to function as a monomer.[1] The central pore of OmpG is wider than other E. coli porins and it is speculated that it may form a non-specific channel for the passive transport of larger oligosaccharides.[1] OmpG adopts two conformations: open and closed. At neutral pH the porin displays an open conformation. However at a more acidic pH the closed conformation is adopted. This closed conformation is a result of OmpG's flexible extracellular loop 6, which folds across the channel blocking the pore opening. The rearrangement of loop 6 appears to be triggered by a pair of histidine residues, which repel one another at acidic pH, resulting in the breakage of neighbouring H-bonds and a lengthening of loop 6 from 10 to 17 residues[2,3]. &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> [2IWW]<br /> [http://en.wikipedia.org/wiki/Outer_membrane_protein_G].<br /> <br /> ==Additional Resources==<br /> Current applications using nanopores for protein detection [https://www.nanoporetech.com/technology/analytes-and-applications-dna-rna-proteins/protein-analysis-]<br /> For additional information, see: Nanobiotechnology Review [http://www.nature.com/nnano/journal/v6/n4/full/nnano.2011.52.html]<br /> &lt;br /&gt;<br /> <br /> ==References==</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1878752 2013-12-20T15:27:15Z

<p>Christina Chisholm: </p> <hr /> <div>OmpG is a member of [[CBI Molecules]] being studied in the [http://www.chem.umass.edu/~chenlab/ Chen Lab] in the &lt;span class=&quot;plainlinks&quot;&gt;[http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program]&lt;/span&gt; at UMass Amherst and on display at the &lt;span class=&quot;plainlinks&quot;&gt;[http://www.molecularplayground.org/ Molecular Playground]&lt;/span&gt;.<br /> <br /> <br /> &lt;Structure load='2GTG' size='500' frame='true' align='right' caption='Outer Membrane Protein G' scene='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/5'&gt;<br /> <br /> <br /> ===Outer Membrane Protein G===<br /> Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection. The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, we utilize the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present. We propose the use of monomeric protein Outer membrane protein G (OmpG) will allow us to tailor and fine tune properties of this pore in detection of analytes. <br /> <br /> This &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/4'&gt;monomeric porin&lt;/scene&gt; has features that can be customized as a sensor component, using protein engineering we can develop this protein to be a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;Location of ligand&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> <br /> <br /> ==More about this Structure==<br /> OmpG is a 14-stranded beta-barrel and in contrast to most porins, appears to function as a monomer.[1] The central pore of OmpG is wider than other E. coli porins and it is speculated that it may form a non-specific channel for the passive transport of larger oligosaccharides.[1] OmpG adopts two conformations: open and closed. At neutral pH the porin displays an open conformation. However at a more acidic pH the closed conformation is adopted. This closed conformation is a result of OmpG's flexible extracellular loop 6, which folds across the channel blocking the pore opening. The rearrangement of loop 6 appears to be triggered by a pair of histidine residues, which repel one another at acidic pH, resulting in the breakage of neighbouring H-bonds and a lengthening of loop 6 from 10 to 17 residues[2,3]. &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> [2IWW]<br /> [http://en.wikipedia.org/wiki/Outer_membrane_protein_G].<br /> <br /> ==Additional Resources==<br /> For additional information, see: Nanobiotechnology Review [http://www.nature.com/nnano/journal/v6/n4/full/nnano.2011.52.html]<br /> &lt;br /&gt;<br /> <br /> ==References==</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1878751 2013-12-20T15:10:58Z

<p>Christina Chisholm: </p> <hr /> <div>One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].<br /> <br /> &lt;Structure load='2GTG' size='500' frame='true' align='right' caption='Outer Membrane Protein G' scene='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/5'&gt;<br /> <br /> <br /> ===Outer Membrane Protein G===<br /> Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection. The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, we utilize the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present. We propose the use of monomeric protein Outer membrane protein G (OmpG) will allow us to tailor and fine tune properties of this pore in detection of analytes. <br /> <br /> This &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/4'&gt;monomeric porin&lt;/scene&gt; has features that can be customized as a sensor component, using protein engineering we can develop this protein to be a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;Location of ligand&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> <br /> <br /> ==More about this Structure==<br /> OmpG is a 14-stranded beta-barrel and in contrast to most porins, appears to function as a monomer.[1] The central pore of OmpG is wider than other E. coli porins and it is speculated that it may form a non-specific channel for the passive transport of larger oligosaccharides.[1] OmpG adopts two conformations: open and closed. At neutral pH the porin displays an open conformation. However at a more acidic pH the closed conformation is adopted. This closed conformation is a result of OmpG's flexible extracellular loop 6, which folds across the channel blocking the pore opening. The rearrangement of loop 6 appears to be triggered by a pair of histidine residues, which repel one another at acidic pH, resulting in the breakage of neighbouring H-bonds and a lengthening of loop 6 from 10 to 17 residues[2,3]. &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> [2IWW]<br /> [http://en.wikipedia.org/wiki/Outer_membrane_protein_G].<br /> <br /> ==Additional Resources==<br /> For additional information, see: Nanobiotechnology Review [http://www.nature.com/nnano/journal/v6/n4/full/nnano.2011.52.html]<br /> &lt;br /&gt;<br /> <br /> ==References==</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1876425 2013-12-17T21:29:42Z

<p>Christina Chisholm: </p> <hr /> <div>Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection. The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present. We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> <br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/4'&gt;Opening of pore&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;Location of ligand&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> <br /> <br /> &lt;Structure load='2GTG' size='500' frame='true' align='right' caption='Outer Membrane Protein G' scene='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/5'&gt;<br /> <br /> <br /> ==About this Structure==<br /> [[2IWW]]<br /> OmpG is a 14-stranded beta-barrel and in contrast to most porins, appears to function as a monomer.[1] The central pore of OmpG is wider than other E. coli porins and it is speculated that it may form a non-specific channel for the passive transport of larger oligosaccharides.[1] OmpG adopts two conformations: open and closed. At neutral pH the porin displays an open conformation. However at a more acidic pH the closed conformation is adopted. This closed conformation is a result of OmpG's flexible extracellular loop 6, which folds across the channel blocking the pore opening. The rearrangement of loop 6 appears to be triggered by a pair of histidine residues, which repel one another at acidic pH, resulting in the breakage of neighbouring H-bonds and a lengthening of loop 6 from 10 to 17 residues(2,3). <br /> <br /> [http://en.wikipedia.org/wiki/Outer_membrane_protein_G].<br /> <br /> <br /> ==References==</div>

Christina Chisholm https://proteopedia.org/index.php?title=Christina_Chisholm/Sandbox1&diff=1856994 2013-10-23T16:31:00Z

<p>Christina Chisholm: </p> <hr /> <div>Welcome to Christina's Sandbox!!! :)<br /> <br /> [http://proteopedia.org/wiki/index.php/CBI_Molecule_Workshop, CBI Molecule Workshop]<br /> <br /> [http://www.umass.edu, UMass Amherst]</div>

Christina Chisholm https://proteopedia.org/index.php?title=Christina_Chisholm/Sandbox1&diff=1856992 2013-10-23T16:29:54Z

<p>Christina Chisholm: </p> <hr /> <div>Welcome to Christina's Sandbox!!! :)<br /> <br /> [http://proteopedia.org/wiki/index.php/CBI_Molecule_Workshop, CBI Molecule Workshop]</div>

Christina Chisholm https://proteopedia.org/index.php?title=Christina_Chisholm/Sandbox1&diff=1856990 2013-10-23T16:29:10Z

<p>Christina Chisholm: </p> <hr /> <div>Welcome to Christina's Sandbox!!! :)<br /> <br /> CBI Molecule Workshop[http://proteopedia.org/wiki/index.php/CBI_Molecule_Workshop]</div>

Christina Chisholm https://proteopedia.org/index.php?title=Christina_Chisholm/Sandbox1&diff=1856989 2013-10-23T16:28:46Z

<p>Christina Chisholm: </p> <hr /> <div>Welcome to Christina's Sandbox!!! :)<br /> <br /> [http://proteopedia.org/wiki/index.php/CBI_Molecule_Workshop]</div>

Christina Chisholm https://proteopedia.org/index.php?title=Christina_Chisholm/Sandbox1&diff=1856988 2013-10-23T16:28:16Z

<p>Christina Chisholm: </p> <hr /> <div>Welcome to Christina's Sandbox!!! :)<br /> <br /> [CBI Molecule Workshop]</div>

Christina Chisholm https://proteopedia.org/index.php?title=Christina_Chisholm/Sandbox1&diff=1856987 2013-10-23T16:27:36Z

<p>Christina Chisholm: </p> <hr /> <div>Welcome to Christina's Sandbox!!! :)<br /> <br /> [CBI Molecule Workshop http://proteopedia.org/wiki/index.php/CBI_Molecule_Workshop]</div>

Christina Chisholm https://proteopedia.org/index.php?title=Christina_Chisholm/Sandbox1&diff=1856982 2013-10-23T16:26:20Z

<p>Christina Chisholm: </p> <hr /> <div>Welcome to Christina's Sandbox!!! :)<br /> <br /> [CBI Molecule Workshop]</div>

Christina Chisholm https://proteopedia.org/index.php?title=Christina_Chisholm/Sandbox1&diff=1856975 2013-10-23T16:24:13Z

<p>Christina Chisholm: New page: Welcome to Christina&#039;s Sandbox!!! :)</p> <hr /> <div>Welcome to Christina's Sandbox!!! :)</div>

Christina Chisholm https://proteopedia.org/index.php?title=CBI_Molecules&diff=1635141 2012-12-17T18:05:26Z

<p>Christina Chisholm: </p> <hr /> <div>These are molecules under study by members of the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program].<br /> Many of the molecules we study are featured at the [http://www.molecularplayground.org/ Molecular Playground] (see also [[Molecular Playground|Molecular Playground in Proteopedia]]). Follow the links below to read nontechnical descriptions, in Proteopedia, of these molecules.<br /> <br /> UMass CBI Members, add your molecules to the list (which is alphabetical by CBI research mentor); follow the instructions below the list.<br /> <br /> Fall 2012: CBI Molecules are due 12/12/12 and should be added at the TOP of the list from your lab. Label it as &quot;in progress&quot; until you are finished. For those editing an existing CBI Molecule, start from that entry so that it retains the full author list of all authors that contributed (or include credits to the original page and authors if it does not -- I may be able to request additions to the author list).<br /> <br /> <br /> ==Molecules==<br /> '''** Designates CBI Molecules Featured on [http://http://www.umass.edu/cbi/ CBI website]'''<br /> <br /> Bhatia Lab<br /> <br /> : '''[[Molecular Playground/Alginate-Fall2011]]''', Joe White, David Griffin<br /> <br /> : '''[[Molecular Playground/Alginate-Fall2010]]''', Joe White, David Griffin<br /> <br /> : '''[[Molecular Playground/Poly(ethylene glycol)]]''', Erika M. Saffer<br /> <br /> <br /> [http://chamberslab.com/wp/ Chambers Lab]<br /> <br /> : '''[[Molecular Playground/Glutamate Receptor]]''', Amanda Hussey, Steve McCarron, Rosie Combs-Bachmann, Mariel Feliciano<br /> <br /> <br /> <br /> [http://www.chem.umass.edu/~chenlab/index.HTML Chen Lab]<br /> <br /> : '''[[Molecular Playground/OmpG]]''', Christina Chisholm<br /> <br /> <br /> [http://openwetware.org/wiki/Chien Chien Lab]<br /> <br /> : **'''[[Molecular Playground/Hexameric ClpX]]''', Joanne Lau <br /> :: Best CBI Molecule 2011<br /> <br /> : '''[[Molecular Playground/DNA replication initiator DnaA]]''', Jing Liu<br /> <br /> <br /> Forbes Lab<br /> <br /> : '''[[Molecular Playground/CheR]]''', Miaomin Zhang<br /> <br /> : '''[[Molecular Playground/RBP]]''', Jan Panteli<br /> <br /> : '''[[Molecular Playground/TRAIL]]''', Charley Swofford<br /> <br /> <br /> [http://www.biochem.umass.edu/garman/index.html Garman Lab]<br /> <br /> : '''[[Molecular Playground/Human Protective Protein Cathepsin A]]''', Yadilette Rivera-Colon<br /> <br /> : '''[[Molecular Playground/Human PPCA]]''', Nilima Kolli<br /> <br /> <br /> [http://people.chem.umass.edu/gieraschlab/ Gierasch Lab]<br /> <br /> : '''[[CRABP I ( Cellular Retinoic Acid Binding Protein )|Molecular Playground/CRABP I]]''', Kristine Faye Pobre, Mylene Ferrolino,Mangai Periasamy<br /> :: Best Overall CBI Molecule 2010<br /> <br /> : '''[[Molecular Playground/CRABP I (Cellular Retinoic Acid Binding Protein)]]''', Gustavo Elberto Epalza Sanchez<br /> (compare this to the previous version above to see what's new)<br /> <br /> : **'''[[Molecular_Playground/DHFR]]''', Karan Hingorani <br /> :: Best CBI Molecule 2012<br /> <br /> <br /> [http://people.chem.umass.edu/jhardy/ Hardy Lab]<br /> <br /> : '''[[Molecular Playground/[[Caspase-3 Regulatory Mechanisms]]''', Scott Eron, Bay Serrano, Yunlong Zhao<br /> <br /> : ''' [[Molecular Playground/Caspase-6 and neurodegeneration]]''', Kevin Buadlart Dagbay<br /> <br /> : '''[[Molecular Playground/Caspase-7 Dynamics]]'''<br /> <br /> : '''[[Molecular Playground/Caspase-9 Regulation]]''', Kristen Huber<br /> <br /> : '''[[Molecular Playground/Caspase-6 (new)]]''', Elih Velazquez<br /> <br /> : '''[[Molecular Playground/Influenza A M2 transmembrane domain]]''', Samantha Nicholls<br /> <br /> : '''[[Molecular Playground/Dengue Virus Protease]]''', Muslum Yildiz<br /> <br /> <br /> Hebert Lab<br /> <br /> : '''[[Molecular_Playground/ERDj5]]''', Lydia Lamriben<br /> : '''[[Molecular Playground/Saposin C]]''', Abla Tannous<br /> : '''[[Molecular_Playground/ERMan1]]''', Johan Sunryd<br /> <br /> <br /> [http://people.biochem.umass.edu/aheuck/aph.html Heuck Lab]<br /> <br /> : '''[[Molecular_Playground/Pcr H]]''', Fabian Romano<br /> <br /> <br /> [http://people.chem.umass.edu/mholden/ Holden Lab]<br /> <br /> : '''[[Molecular Playground/Protective Antigen]]''', Jing Huang<br /> <br /> <br /> <br /> [http://www.chem.umass.edu/people/kaltashovlab/ Kaltashov Lab]<br /> <br /> : ''' [[Molecular Playground/Transferrin]]''', Khaja Muneeruddin, Jake Pawlowski<br /> <br /> : '''[[Molecular Playground/Velaglucerase]]''', Adriana Kita<br /> <br /> <br /> <br /> Knapp lab<br /> <br /> :'''[[Molecular Playground/Prolyl Hydroxylase Domain (PHD) Enzyme]]''', Cristina Martin, Serap Pektas<br /> :: Best CBI Molecule Proteopedia Page 2010<br /> <br /> : '''[[Molecular Playground/FIH]]''', Cornelius Taabazuing, Breanne Holmes, John Hangasky<br /> <br /> <br /> [http://people.chem.umass.edu/mmaroney/ Maroney Lab]<br /> <br /> : New Fall 2012!! '''[[Molecular Playground/Nickel Superoxide Dismutase]]''', Carolyn Carr<br /> : '''[[Molecular Playground/CsoR and RcnR]]''', Heidi Hu<br /> : New Fall 2012!! '''[[Molecular Playground/HypA]]''', Heidi Hu<br /> <br /> <br /> [http://www.chem.umass.edu/~cmartin/ Martin Lab]<br /> <br /> : **'''[[Molecular Playground/T7 RNAP Conformations]]''', Luis E. Ramirez-Tapia <br /> :: Best CBI Molecule 2011<br /> : '''[[Molecular Playground/T7 RNA Polymerase (7 mer int)]]''', Ankit Vahia<br /> <br /> : '''[[Molecular Playground/Human mtRNA pol]]''', Ketan Mathavan <br /> <br /> <br /> Peyton Lab<br /> : '''[[Molecular Playground/C-Raf]]''', Thuy Nguyen<br /> : '''[[Molecular Playground/FAK]]''', Dannielle Ryman<br /> <br /> <br /> [http://roberts.openwetware.org/ Roberts Lab]<br /> <br /> : '''[[Molecular Playground/Taxol]]''', Rohan Patil, Sarah Wilson<br /> <br /> : '''[[Molecular Playground/Insulin]]''', Whitney Stoppel<br /> <br /> <br /> [http://www.umass.edu/rotellogroup/ Rotello Lab]<br /> <br /> : '''[[Reverse transcriptase|Molecular Playground/Reverse Transcriptase]]''', Daniel Moyano-Marino<br /> <br /> : '''[[Molecular Playground/Pancreatic Lipase]]''', Rui Tang<br /> <br /> : '''[[Molecular playground/Chymotrypsin]]''', Brad<br /> <br /> : '''[[Molecular Playground/Targeting Peptide]]''', David Solfiell<br /> <br /> <br /> <br /> [https://elements.chem.umass.edu/schnarrlab/ Schnarr Lab] <br /> <br /> : '''[[Molecular Playground/4'-PHOSPHOPANTETHEINYL TRANSFERASE (Sfp)]]''', Jon Amoroso, Gitanjeli Prasad, Lawrence Sheringham Borketey <br /> <br /> : '''[[6-deoxyerythronolide_B_synthase_(DEBS)|Molecular Playground/6-Deoxyerythronolide B Synthase]]''', Tsung-Yi Lin, Jon Amoroso<br /> <br /> : '''[[Molecular Playground/ACP apo]]''', Gitanjeli Prasad<br /> <br /> <br /> Tew Lab<br /> <br /> : '''[[Molecular Playground/HIV Tat]]''', Brittany deRonde<br /> <br /> <br /> Thayumanavan Lab<br /> <br /> : '''[[Molecular Playground/Lysozyme ]]''', Daniella Gonzalez<br /> <br /> : '''[[Molecular Playground/Beta-galactosidase]]''', Judy Ventura<br /> <br /> : '''[[User:Krishna Reddy Ragupathi|Molecular Playground/Carbonic Anhydrase]]''', Krishna Reddy Raghupathi<br /> <br /> : '''[[User:Rami Rajasekhar Reddy|Molecular Playground/Avidin]]''', Rami Rajasekar Reddy<br /> <br /> : '''[[Molecular Playground/Biotin binding avidin]]''', Diego Amado <br /> <br /> : '''[[User:Jiaming Zhuang|Molecular Playground/MMP12]]''', Jiaming Zhuang<br /> <br /> : ''' [[User:Jing Guo|Molecular Playground/Gluconase]]''', Jing Guo<br /> <br /> : '''[[Molecular Playground/Glutathione Reductase]]''', Reuben Chacko<br /> <br /> <br /> Thayumanavan &amp; Vachet Labs<br /> <br /> : '''[[Molecular Playground/Trypsin]]''', Gladys Murage<br /> <br /> <br /> [http://people.chem.umass.edu/thompson/index.html Thompson] &amp; [http://www.chem.umass.edu/~rmweis/weislab/ Weis] Labs<br /> <br /> : '''[[Molecular Playground/CheA]]''', Elizabeth R. Haglin<br /> <br /> : '''[[Molecular Playground/Bacterial Chemotaxis Receptors]]''', Lynmarie K. Thompson, Shiela M. Jones<br /> <br /> : '''[[Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor]]''', Meili Yang<br /> <br /> : '''[[Molecular Playground/Cytoplasmic domain of chemoreceptor of Thermotoga maritima]]''', Xuni Li<br /> <br /> <br /> [http://www.chem.umass.edu/~vachet/index.html Vachet Lab]<br /> <br /> : '''[[Molecular playground/beta 2 microglobulin]]''', Nick Borotto<br /> :: Best CBI Molecule Jmol scenes 2010<br /> <br /> : '''[[Molecular Playground/Myoglobin]]''', Yuping Zhou <br /> <br /> :'''[[Molecular Playground/ Copper-Zinc Superoxide Dismutase]]''', Shaynah Browne<br /> <br /> <br /> <br /> Other Molecules of interest<br /> <br /> : '''[[Molecular Playground/PcrA Helicase]]''', Luis E Ramirez-Tapia, [http://www.chem.umass.edu/~cmartin/ Martin Lab]<br /> <br /> <br /> Other Laboratories<br /> <br /> : '''[[Molecular Playground/YKL-40]]''', Ralph A. Francescone III, [http://www.bio.umass.edu/mcb/faculty/Shao.html Shao Lab]<br /> <br /> : '''[[Molecular Playground/BLG|Molecular Playground/β-lactoglobulin]]''', Daniel Seeman, Dubin Lab<br /> <br /> : '''[[Molecular Playground/ADAM13]]''', Genevieve Abbruzzese, Alfandari Lab<br /> <br /> ==Instructions==<br /> <br /> '''Congratulations to the prize-winning CBI molecules noted above! The new goal is for students to work collaboratively to create one excellent CBI Molecule for each CBI research group, to be featured on the CBI website.'''<br /> <br /> Fall 2012: Complete steps 1-3 by 10/10/12, in preparation for the CBI Molecule Workshop.<br /> <br /> 1. If you don't already have one, request a Proteopedia account and log in. <br /> <br /> 2. Get started working in Proteopedia by using the links at [[Help:Contents]]. Make yourself a sandbox page: Enter &quot;User:Your Name/Sandbox 1&quot; (omit quotes) in the search box, then follow instructions to edit this page. Practice entering text, inserting a structure window with scrolling text (green 4-square button on the right), and creating a green scene. You can look at other Proteopedia pages in edit mode to see how different effects (like colored text) are achieved (but this won't show you how the scene effects are made). <br /> <br /> 3. Get together with the other Chalk Talk students in your research group and decide which molecule you will improve or create. Develop ideas for the scenes you wish to show. You will work on these during the workshop with our help, and then finish them on your own.<br /> <br /> You are encouraged to collaborate on this year's CBI Molecules, but everyone will need to do some editing of the molecule so that they each appear as authors on the final list. If you are the sole student from your group enrolled in Chalk Talk and have not previously made a CBI Molecule, try to convince another group member who has previously made a CBI Molecule (see list above) to join us for the workshop so that you can work together.<br /> <br /> A successful CBI Molecule will be an interesting, nontechnical description of a molecule related to your group's research. It should not be super long, but instead have multiple green scenes. Green scenes should clearly show an interesting feature and should be attractive. Use the green scenes to help you make interesting points about the molecule (do not try to describe every feature of the molecule). It's great if you can end with a brief statement about how it relates to your group's research goals.<br /> <br /> 4. Your final pages should be called &quot;Molecular Playground/your molecule&quot; and should have links on this CBI Molecule page -- put the new ones first on the list from your research group. Label them &quot;in progress&quot; until you are finished.<br /> <br /> ==Links to HELP pages==<br /> Overview at [[Help:Contents ]]<br /> <br /> See also [[Help:Getting_Started_in_Proteopedia]] <br /> <br /> Videos showing how to use Proteopedia:<br /> [[Proteopedia:Video_Guide]]<br /> (Sometimes slow -- if you pause the video and wait awhile it will download and then you can play it without interruptions)<br /> <br /> [[Proteopedia:DIY:Scenes|Proteopedia Scenes: Do It Yourself]]<br /> gives succinct step by step instructions on how to create a molecular scene.<br /> <br /> A powerpoint-like set of slides that walks a user through the process of creating a new page and a new molecular scene/green link.<br /> [http://www.proteopedia.org/wiki/images/1/1b/2009_07_13_Proteopedia_Workshop.pdf Proteopedia Workshop Slides]<br /> <br /> [[Proteopedia:Guidelines for Ethical Writing]].<br /> Please pay attention to the section about images. There are links to examples of images re-used with explicit permission.<br /> <br /> For other help resources, click on [[Help:Contents|Help]] in the ''navigation'' box at the upper left of every page in Proteopedia.</div>

Christina Chisholm https://proteopedia.org/index.php?title=User:Christina_Chisholm/Sandbox_1&diff=1635140 2012-12-17T18:04:31Z

<p>Christina Chisholm: User:Christina Chisholm/Sandbox 1 moved to Molecular Playground/OmpG: make public</p> <hr /> <div>#REDIRECT [[Molecular Playground/OmpG]]</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1635139 2012-12-17T18:04:31Z

<p>Christina Chisholm: User:Christina Chisholm/Sandbox 1 moved to Molecular Playground/OmpG: make public</p> <hr /> <div>Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection. The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present. We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> <br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/4'&gt;Opening of pore&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;Location of ligand&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> <br /> <br /> &lt;Structure load='2GTG' size='500' frame='true' align='right' caption='Outer Membrane Protein G' scene='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/5'&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1632893 2012-12-12T21:27:56Z

<p>Christina Chisholm: </p> <hr /> <div>Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection. The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present. We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> <br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/4'&gt;Opening of pore&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;Location of ligand&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> <br /> <br /> &lt;Structure load='2GTG' size='500' frame='true' align='right' caption='Outer Membrane Protein G' scene='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/5'&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1632796 2012-12-12T21:25:53Z

<p>Christina Chisholm: </p> <hr /> <div>Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection. The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present. We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> <br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/4'&gt;Opening of pore&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;Location of ligand&lt;/scene&gt;<br /> <br /> <br /> &lt;Structure load='2GTG' size='500' frame='true' align='right' caption='Outer Membrane Protein G' scene='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/5'&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1632484 2012-12-12T21:19:10Z

<p>Christina Chisholm: </p> <hr /> <div>Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection. The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present. We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> <br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/4'&gt;Opening of pore&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;Location of ligand&lt;/scene&gt;<br /> <br /> <br /> &lt;Structure load='2GTG' size='500' frame='true' align='right' caption='Outer Membrane Protein G' scene='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1632313 2012-12-12T21:15:33Z

<p>Christina Chisholm: </p> <hr /> <div>Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection. The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present. We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> <br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/4'&gt;Opening of pore&lt;/scene&gt;<br /> <br /> <br /> &lt;Structure load='2GTG' size='500' frame='true' align='right' caption='Outer Membrane Protein G' scene='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1631854 2012-12-12T21:05:38Z

<p>Christina Chisholm: </p> <hr /> <div>Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection. The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present. We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;&lt;/scene&gt;<br /> <br /> <br /> &lt;Structure load='2GTG' size='500' frame='true' align='right' caption='Outer Membrane Protein G' scene='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1631833 2012-12-12T20:54:51Z

<p>Christina Chisholm: </p> <hr /> <div>Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection. The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present. We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. <br /> <br /> <br /> &lt;Structure load='2GTG' size='500' frame='true' align='right' caption='Outer Membrane Protein G' scene='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1631787 2012-12-12T20:52:22Z

<p>Christina Chisholm: </p> <hr /> <div>Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection. The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present. We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. <br /> <br /> <br /> &lt;Structure load='2GTG' size='500' frame='true' align='right' caption='Insert caption here' scene='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1631582 2012-12-12T20:49:19Z

<p>Christina Chisholm: </p> <hr /> <div>Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection. The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present. We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. <br /> <br /> <br /> &lt;Structure load='2GTG' size='500' frame='true' align='right' caption='Insert caption here' scene='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1631526 2012-12-12T20:48:18Z

<p>Christina Chisholm: </p> <hr /> <div>Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection (1). The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present (2). We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. <br /> <br /> <br /> &lt;Structure load='2GTG' size='500' frame='true' align='right' caption='Insert caption here' scene='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt; <br /> <br /> <br /> <br /> <br /> &lt;applet load='3spa' size='[450,338]' frame='true' align='right'<br /> caption='Outer Membrane Protein G' scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;&lt;/scene&gt;<br /> <br /> ====References====</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1631421 2012-12-12T20:40:46Z

<p>Christina Chisholm: </p> <hr /> <div><br /> Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection (1). The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present (2). We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. <br /> <br /> <br /> <br /> <br /> <br /> &lt;applet load='3spa' size='[450,338]' frame='true' align='right'<br /> caption='Outer Membrane Protein G' scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;&lt;/scene&gt;<br /> <br /> ====References====</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1631416 2012-12-12T20:39:25Z

<p>Christina Chisholm: </p> <hr /> <div><br /> <br /> <br /> Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection (1). The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present (2). We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. <br /> <br /> <br /> <br /> <br /> <br /> &lt;applet load='3spa' size='[450,338]' frame='true' align='right'<br /> caption='Outer Membrane Protein G' &lt;scene name='User:User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/1'&gt;&gt;<br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;&lt;/scene&gt;<br /> <br /> ====References====</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1631415 2012-12-12T20:39:10Z

<p>Christina Chisholm: </p> <hr /> <div><br /> {{Clear}}<br /> <br /> <br /> ==Engineering Outer Membrane Protein as a Stochastic Sensor==&lt;StructureSection load= &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/2'&gt;TextToBeDisplayed&lt;/scene&gt;size='500' side='right'<br /> ========== <br /> <br /> <br /> Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection (1). The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present (2). We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. <br /> <br /> <br /> <br /> <br /> <br /> &lt;applet load='3spa' size='[450,338]' frame='true' align='right'<br /> caption='Outer Membrane Protein G' &lt;scene name='User:User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/1'&gt;&gt;<br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;&lt;/scene&gt;<br /> <br /> ====References====</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1631286 2012-12-12T20:33:59Z

<p>Christina Chisholm: </p> <hr /> <div><br /> <br /> {{Clear}}<br /> <br /> <br /> ==Engineering Outer Membrane Protein as a Stochastic Sensor==&lt;StructureSection load='1acj' size='500' side='right' caption='Crystal Structure of tacrine bound to acetylcholinesterase [[1acj]] ' scene=&gt;Anything in this section will appear adjacent to the 3D structure and will be scrollable.<br /> <br /> <br /> ========== <br /> <br /> <br /> Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection (1). The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present (2). We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. <br /> <br /> <br /> <br /> <br /> <br /> &lt;applet load='3spa' size='[450,338]' frame='true' align='right'<br /> caption='Outer Membrane Protein G' scene='User:User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/1'&gt;&gt;<br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;&lt;/scene&gt;<br /> <br /> ====Refrences====</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1631260 2012-12-12T20:31:49Z

<p>Christina Chisholm: </p> <hr /> <div>[[Image:intactModelLargeText.jpg|frame|Bacterial chemotaxis receptor]]<br /> <br /> Many bacteria can &quot;smell&quot; their surroundings and &quot;choose&quot; where to go. They detect molecules such as amino acids or sugars using receptors that bind these molecules and transmit a signal into the cell. This signal controls several proteins which ultimately control the motors that rotate the flagella to cause the cell to either continue swimming or to tumble. When an attractant molecule binds, it signals: &quot;Things look good, keep swimming!&quot; The opposite signal occurs when bacteria sense decreasing concentrations of attractant molecules: &quot;Time to tumble and try a new swimming direction.&quot;<br /> <br /> <br /> A bacterial chemotaxis receptor is an unusually long alpha-helical structure. The attractant molecule (the ligand) binds near the top of this picture and sends a signal across the membrane into the cell to control proteins that bind near the bottom. This is a model of the structure of the receptor based on experimental structures of pieces of related proteins.<br /> <br /> <br /> &lt;applet load='1wat' size='[450,338]' frame='true' align='left'<br /> caption='Aspartate receptor ligand binding domain (1wat)' scene='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4'/&gt;<br /> <br /> <br /> === Ligand-binding domain ===<br /> <br /> <br /> <br /> The spinning protein (&lt;scene name='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4'&gt;Initial view&lt;/scene&gt;) ) is the ligand binding domain of the aspartate receptor with the aspartate ligand bound (LKT).<br /> <br /> <br /> Molecular Playground banner: A receptor protein used by bacteria to &quot;smell&quot; their environment.<br /> <br /> {{Clear}}<br /> <br /> <br /> ==Using the new scrollable sections==&lt;StructureSection load='1acj' size='500' side='right' caption='Crystal Structure of tacrine bound to acetylcholinesterase [[1acj]] ' scene=&gt;Anything in this section will appear adjacent to the 3D structure and will be scrollable.<br /> <br /> <br /> =====Engineering Outer Membrane Protein as a Stochastic Sensor===== <br /> <br /> <br /> Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection (1). The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present (2). We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. <br /> <br /> <br /> <br /> <br /> <br /> &lt;applet load='3spa' size='[450,338]' frame='true' align='right'<br /> caption='Outer Membrane Protein G' scene='User:User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/1'&gt;&gt;<br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;&lt;/scene&gt;<br /> <br /> ====Refrences====</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1631194 2012-12-12T20:12:50Z

<p>Christina Chisholm: </p> <hr /> <div><br /> =====Engineering Outer Membrane Protein as a Stochastic Sensor===== <br /> <br /> <br /> Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection (1). The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present (2). We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. <br /> <br /> <br /> <br /> <br /> <br /> &lt;applet load='3spa' size='[450,338]' frame='true' align='right'<br /> caption='Outer Membrane Protein G' scene='User:User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/1'&gt;&gt;<br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;&lt;/scene&gt;<br /> <br /> ====Refrences====</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1631186 2012-12-12T20:04:06Z

<p>Christina Chisholm: </p> <hr /> <div>Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection (1). The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present (2). We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. <br /> <br /> <br /> <br /> <br /> <br /> {{Clear}}<br /> &lt;applet load='3spa' size='[450,338]' frame='true' align='right'<br /> caption='Outer Membrane Protein G' scene='User:User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/1'&gt;&gt;<br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;&lt;/scene&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1631185 2012-12-12T20:01:59Z

<p>Christina Chisholm: </p> <hr /> <div>Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection (1). The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present (2). We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. <br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> <br /> <br /> {{Clear}}<br /> &lt;applet load='3spa' size='[450,338]' frame='true' align='right'<br /> caption='Outer Membrane Protein G' scene='User:User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/1'&gt;&gt;<br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/1'&gt;default&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;&lt;/scene&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=User:Christina_Chisholm&diff=1631184 2012-12-12T19:56:52Z

<p>Christina Chisholm: </p> <hr /> <div>*[[User:Christina Chisholm/Sandbox 1]]<br /> <br /> * Full Real Name: Christina Chisholm<br /> <br /> * Position:Graduate Student<br /> <br /> * Institution :University of Massachusetts Amherst<br /> <br /> * City, State/Province, Country:Amherst, Massachusetts, USA<br /> <br /> * Field of Expertise or Study: Biochemistry</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1631181 2012-12-12T19:55:40Z

<p>Christina Chisholm: /* OmpG */</p> <hr /> <div>Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection (1). The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present (2). We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. <br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> <br /> === OmpG ===<br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/1'&gt;default&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;TextToBeDisplayed&lt;/scene&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1631179 2012-12-12T19:54:38Z

<p>Christina Chisholm: </p> <hr /> <div>Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection (1). The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present (2). We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. <br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> <br /> === OmpG ===<br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/1'&gt;default&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> <br /> <br /> <br /> {{Clear}}<br /> <br /> <br /> ==Using the new scrollable sections==&lt;StructureSection load='1acj' size='500' side='right' caption='Crystal Structure of tacrine bound to acetylcholinesterase [[1acj]] ' scene=&gt;Anything in this section will appear adjacent to the 3D structure and will be scrollable.<br /> <br /> Use the 4 green squares button (top right in edit mode) to insert a structure window with a companion scrolling text section.<br /> <br /> Here is a &lt;scene name='User:Lynmarie_K_Thompson/Sandbox_1/Tacrine/1'&gt;green scene&lt;/scene&gt; made following the DIY instructions: [[Proteopedia:DIY:Scenes]]<br /> <br /> &lt;/StructureSection&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1631178 2012-12-12T19:51:31Z

<p>Christina Chisholm: </p> <hr /> <div><br /> Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection (1). The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present (2). We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Utilizing the flexibility of an extracellular loop, we will append a ligand to help detect our target analyte. <br /> <br /> &lt;applet load='1wat' size='[450,338]' frame='true' align='left'<br /> caption='Aspartate receptor ligand binding domain (1wat)' scene='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4'/&gt;<br /> <br /> <br /> === OmpG ===<br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/1'&gt;default&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> <br /> Molecular Playground banner: A receptor protein used by bacteria to &quot;smell&quot; their environment.<br /> <br /> {{Clear}}<br /> <br /> <br /> ==Using the new scrollable sections==&lt;StructureSection load='1acj' size='500' side='right' caption='Crystal Structure of tacrine bound to acetylcholinesterase [[1acj]] ' scene=&gt;Anything in this section will appear adjacent to the 3D structure and will be scrollable.<br /> <br /> Use the 4 green squares button (top right in edit mode) to insert a structure window with a companion scrolling text section.<br /> <br /> Here is a &lt;scene name='User:Lynmarie_K_Thompson/Sandbox_1/Tacrine/1'&gt;green scene&lt;/scene&gt; made following the DIY instructions: [[Proteopedia:DIY:Scenes]]<br /> <br /> &lt;/StructureSection&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1631176 2012-12-12T19:48:53Z

<p>Christina Chisholm: </p> <hr /> <div>[[Image:intactModelLargeText.jpg|frame|Bacterial chemotaxis receptor]]<br /> <br /> Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection (1). The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present (2). We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Furthermore, an OmpG sensing library could be built for the screening of constructs/ analytes according to their ability to recognize specific targets of medical relevance. <br /> <br /> <br /> <br /> &lt;applet load='1wat' size='[450,338]' frame='true' align='left'<br /> caption='Aspartate receptor ligand binding domain (1wat)' scene='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4'/&gt;<br /> <br /> <br /> === OmpG ===<br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/1'&gt;default&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> <br /> Molecular Playground banner: A receptor protein used by bacteria to &quot;smell&quot; their environment.<br /> <br /> {{Clear}}<br /> <br /> <br /> ==Using the new scrollable sections==&lt;StructureSection load='1acj' size='500' side='right' caption='Crystal Structure of tacrine bound to acetylcholinesterase [[1acj]] ' scene=&gt;Anything in this section will appear adjacent to the 3D structure and will be scrollable.<br /> <br /> Use the 4 green squares button (top right in edit mode) to insert a structure window with a companion scrolling text section.<br /> <br /> Here is a &lt;scene name='User:Lynmarie_K_Thompson/Sandbox_1/Tacrine/1'&gt;green scene&lt;/scene&gt; made following the DIY instructions: [[Proteopedia:DIY:Scenes]]<br /> <br /> &lt;/StructureSection&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1631174 2012-12-12T19:44:23Z

<p>Christina Chisholm: /* Ligand-binding domain */</p> <hr /> <div>[[Image:intactModelLargeText.jpg|frame|Bacterial chemotaxis receptor]]<br /> <br /> Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection (1). The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present (2). We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Furthermore, an OmpG sensing library could be built for the screening of constructs/ analytes according to their ability to recognize specific targets of medical relevance. <br /> <br /> <br /> <br /> &lt;applet load='1wat' size='[450,338]' frame='true' align='left'<br /> caption='Aspartate receptor ligand binding domain (1wat)' scene='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4'/&gt;<br /> <br /> <br /> === Ligand-binding domain ===<br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/1'&gt;default&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/1'&gt;224&lt;/scene&gt;<br /> <br /> The spinning protein Christina_Chisholm/Sandbox_1/224highlighted_ompg/5'&gt;TextToBeDisplayed&lt;/scene&gt; displays the location where ligand will be appended onto OmpG.<br /> <br /> Molecular Playground banner: A receptor protein used by bacteria to &quot;smell&quot; their environment.<br /> <br /> {{Clear}}<br /> <br /> <br /> ==Using the new scrollable sections==&lt;StructureSection load='1acj' size='500' side='right' caption='Crystal Structure of tacrine bound to acetylcholinesterase [[1acj]] ' scene=&gt;Anything in this section will appear adjacent to the 3D structure and will be scrollable.<br /> <br /> Use the 4 green squares button (top right in edit mode) to insert a structure window with a companion scrolling text section.<br /> <br /> Here is a &lt;scene name='User:Lynmarie_K_Thompson/Sandbox_1/Tacrine/1'&gt;green scene&lt;/scene&gt; made following the DIY instructions: [[Proteopedia:DIY:Scenes]]<br /> <br /> &lt;/StructureSection&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1631170 2012-12-12T19:41:26Z

<p>Christina Chisholm: </p> <hr /> <div>[[Image:intactModelLargeText.jpg|frame|Bacterial chemotaxis receptor]]<br /> <br /> Protein biosensors serve as an analytical device combining a biological component with a physiochemical detector. Through protein engineering we are able to utilize pores to be used as stochastic sensors, for single molecule detection (1). The applications of biosensors range from fundamental research, clinical diagnosis, and even advances in homeland security. PCR (Polymerase chain reaction) and ELISA (Enzyme- linked immunosorbent assay) are current sensitive detection methods. However, these methods are time consuming and require laborious effort, where results are provided hours or days later. For this reason alternate approaches are mounting in demands that are rapid in detection time, highly sensitive and reliable. <br /> <br /> Through stochastic sensing, utilizes the passage of ionic current through a protein pore containing engineered recognition sites, allowing for monitoring of analytes present (2). We propose the use of monomeric protein OmpG (outer membrane protein G) will allow us to tailor and fine tune properties of this pore in detection of analytes. This monomeric porin has features, which allow for complex properties to be customized as a sensor compartment, via protein engineering, providing eminent potential for the development of this protein as a successful biosensor. Furthermore, an OmpG sensing library could be built for the screening of constructs/ analytes according to their ability to recognize specific targets of medical relevance. <br /> <br /> <br /> <br /> &lt;applet load='1wat' size='[450,338]' frame='true' align='left'<br /> caption='Aspartate receptor ligand binding domain (1wat)' scene='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4'/&gt;<br /> <br /> <br /> === Ligand-binding domain ===<br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/1'&gt;default&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/1'&gt;224&lt;/scene&gt;<br /> <br /> The spinning protein (&lt;scene name='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4'&gt;Initial view&lt;/scene&gt;) ) is the ligand binding domain of the aspartate receptor with the aspartate ligand bound (LKT).<br /> <br /> <br /> Molecular Playground banner: A receptor protein used by bacteria to &quot;smell&quot; their environment.<br /> <br /> {{Clear}}<br /> <br /> <br /> ==Using the new scrollable sections==&lt;StructureSection load='1acj' size='500' side='right' caption='Crystal Structure of tacrine bound to acetylcholinesterase [[1acj]] ' scene=&gt;Anything in this section will appear adjacent to the 3D structure and will be scrollable.<br /> <br /> Use the 4 green squares button (top right in edit mode) to insert a structure window with a companion scrolling text section.<br /> <br /> Here is a &lt;scene name='User:Lynmarie_K_Thompson/Sandbox_1/Tacrine/1'&gt;green scene&lt;/scene&gt; made following the DIY instructions: [[Proteopedia:DIY:Scenes]]<br /> <br /> &lt;/StructureSection&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1543580 2012-10-10T17:32:29Z

<p>Christina Chisholm: </p> <hr /> <div>[[Image:intactModelLargeText.jpg|frame|Bacterial chemotaxis receptor]]<br /> <br /> Many bacteria can &quot;smell&quot; their surroundings and &quot;choose&quot; where to go. They detect molecules such as amino acids or sugars using receptors that bind these molecules and transmit a signal into the cell. This signal controls several proteins which ultimately control the motors that rotate the flagella to cause the cell to either continue swimming or to tumble. When an attractant molecule binds, it signals: &quot;Things look good, keep swimming!&quot; The opposite signal occurs when bacteria sense decreasing concentrations of attractant molecules: &quot;Time to tumble and try a new swimming direction.&quot;<br /> <br /> <br /> A bacterial chemotaxis receptor is an unusually long alpha-helical structure. The attractant molecule (the ligand) binds near the top of this picture and sends a signal across the membrane into the cell to control proteins that bind near the bottom. This is a model of the structure of the receptor based on experimental structures of pieces of related proteins.<br /> <br /> <br /> &lt;applet load='1wat' size='[450,338]' frame='true' align='left'<br /> caption='Aspartate receptor ligand binding domain (1wat)' scene='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4'/&gt;<br /> <br /> <br /> === Ligand-binding domain ===<br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/1'&gt;default&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/1'&gt;224&lt;/scene&gt;<br /> <br /> The spinning protein (&lt;scene name='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4'&gt;Initial view&lt;/scene&gt;) ) is the ligand binding domain of the aspartate receptor with the aspartate ligand bound (LKT).<br /> <br /> <br /> Molecular Playground banner: A receptor protein used by bacteria to &quot;smell&quot; their environment.<br /> <br /> {{Clear}}<br /> <br /> <br /> ==Using the new scrollable sections==&lt;StructureSection load='1acj' size='500' side='right' caption='Crystal Structure of tacrine bound to acetylcholinesterase [[1acj]] ' scene=&gt;Anything in this section will appear adjacent to the 3D structure and will be scrollable.<br /> <br /> Use the 4 green squares button (top right in edit mode) to insert a structure window with a companion scrolling text section.<br /> <br /> Here is a &lt;scene name='User:Lynmarie_K_Thompson/Sandbox_1/Tacrine/1'&gt;green scene&lt;/scene&gt; made following the DIY instructions: [[Proteopedia:DIY:Scenes]]<br /> <br /> &lt;/StructureSection&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1543578 2012-10-10T17:29:37Z

<p>Christina Chisholm: </p> <hr /> <div>[[Image:intactModelLargeText.jpg|frame|Bacterial chemotaxis receptor]]<br /> <br /> Many bacteria can &quot;smell&quot; their surroundings and &quot;choose&quot; where to go. They detect molecules such as amino acids or sugars using receptors that bind these molecules and transmit a signal into the cell. This signal controls several proteins which ultimately control the motors that rotate the flagella to cause the cell to either continue swimming or to tumble. When an attractant molecule binds, it signals: &quot;Things look good, keep swimming!&quot; The opposite signal occurs when bacteria sense decreasing concentrations of attractant molecules: &quot;Time to tumble and try a new swimming direction.&quot;<br /> <br /> <br /> A bacterial chemotaxis receptor is an unusually long alpha-helical structure. The attractant molecule (the ligand) binds near the top of this picture and sends a signal across the membrane into the cell to control proteins that bind near the bottom. This is a model of the structure of the receptor based on experimental structures of pieces of related proteins.<br /> <br /> <br /> &lt;applet load='1wat' size='[450,338]' frame='true' align='left'<br /> caption='Aspartate receptor ligand binding domain (1wat)' scene='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4'/&gt;<br /> <br /> <br /> === Ligand-binding domain ===<br /> <br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/1'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> &lt;scene name='User:Christina_Chisholm/Sandbox_1/224highlighted_ompg/1'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> The spinning protein (&lt;scene name='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4'&gt;Initial view&lt;/scene&gt;) ) is the ligand binding domain of the aspartate receptor with the aspartate ligand bound (LKT).<br /> <br /> <br /> Molecular Playground banner: A receptor protein used by bacteria to &quot;smell&quot; their environment.<br /> <br /> {{Clear}}<br /> <br /> <br /> ==Using the new scrollable sections==&lt;StructureSection load='1acj' size='500' side='right' caption='Crystal Structure of tacrine bound to acetylcholinesterase [[1acj]] ' scene=&gt;Anything in this section will appear adjacent to the 3D structure and will be scrollable.<br /> <br /> Use the 4 green squares button (top right in edit mode) to insert a structure window with a companion scrolling text section.<br /> <br /> Here is a &lt;scene name='User:Lynmarie_K_Thompson/Sandbox_1/Tacrine/1'&gt;green scene&lt;/scene&gt; made following the DIY instructions: [[Proteopedia:DIY:Scenes]]<br /> <br /> &lt;/StructureSection&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=File:2IWW_noBchain.pdb&diff=1543561 2012-10-10T17:17:14Z

<p>Christina Chisholm: </p> <hr /> <div></div>

Christina Chisholm https://proteopedia.org/index.php?title=Molecular_Playground/OmpG&diff=1543538 2012-10-10T16:54:14Z

<p>Christina Chisholm: New page: Bacterial chemotaxis receptor Many bacteria can &quot;smell&quot; their surroundings and &quot;choose&quot; where to go. They detect molecules such as amino acids or ...</p> <hr /> <div>[[Image:intactModelLargeText.jpg|frame|Bacterial chemotaxis receptor]]<br /> <br /> Many bacteria can &quot;smell&quot; their surroundings and &quot;choose&quot; where to go. They detect molecules such as amino acids or sugars using receptors that bind these molecules and transmit a signal into the cell. This signal controls several proteins which ultimately control the motors that rotate the flagella to cause the cell to either continue swimming or to tumble. When an attractant molecule binds, it signals: &quot;Things look good, keep swimming!&quot; The opposite signal occurs when bacteria sense decreasing concentrations of attractant molecules: &quot;Time to tumble and try a new swimming direction.&quot;<br /> <br /> <br /> A bacterial chemotaxis receptor is an unusually long alpha-helical structure. The attractant molecule (the ligand) binds near the top of this picture and sends a signal across the membrane into the cell to control proteins that bind near the bottom. This is a model of the structure of the receptor based on experimental structures of pieces of related proteins.<br /> <br /> <br /> &lt;applet load='1wat' size='[450,338]' frame='true' align='left'<br /> caption='Aspartate receptor ligand binding domain (1wat)' scene='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4'/&gt;<br /> <br /> <br /> === Ligand-binding domain ===<br /> <br /> <br /> <br /> The spinning protein (&lt;scene name='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4'&gt;Initial view&lt;/scene&gt;) ) is the ligand binding domain of the aspartate receptor with the aspartate ligand bound (LKT).<br /> <br /> <br /> Molecular Playground banner: A receptor protein used by bacteria to &quot;smell&quot; their environment.<br /> <br /> {{Clear}}<br /> <br /> <br /> ==Using the new scrollable sections==&lt;StructureSection load='1acj' size='500' side='right' caption='Crystal Structure of tacrine bound to acetylcholinesterase [[1acj]] ' scene=&gt;Anything in this section will appear adjacent to the 3D structure and will be scrollable.<br /> <br /> Use the 4 green squares button (top right in edit mode) to insert a structure window with a companion scrolling text section.<br /> <br /> Here is a &lt;scene name='User:Lynmarie_K_Thompson/Sandbox_1/Tacrine/1'&gt;green scene&lt;/scene&gt; made following the DIY instructions: [[Proteopedia:DIY:Scenes]]<br /> <br /> &lt;/StructureSection&gt;</div>

Christina Chisholm https://proteopedia.org/index.php?title=User:Christina_Chisholm&diff=1543530 2012-10-10T16:51:14Z

<p>Christina Chisholm: </p> <hr /> <div>*[[User:Christina Chisholm/Sandbox 1]]<br /> <br /> * Full Real Name: Christina Chisholm<br /> <br /> * Position:Graduate Student<br /> <br /> * Institution (NO ABBREVIATIONS):University of Massachusetts Amherst<br /> <br /> * City, State/Province, Country:Amherst, Massachusetts, USA<br /> <br /> * Field of Expertise or Study: Biochemistry</div>

Christina Chisholm