Proteopedia - User contributions [en]

CBI Molecules

2011-05-04T14:01:00Z

Shaynah Browne:

These are molecules under study by members of the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program].
Many of the molecules we study are featured at the [http://www.molecularplayground.org/ Molecular Playground]. Follow the links below to read nontechnical descriptions in Proteopedia.

UMass CBI Members, add your molecules to the list (which is alphabetical by CBI research mentor); follow the instructions below the list.

It's great to build on a previous entry, but you must leave the earlier one intact and make a copy that you improve and mark as new. Later we will retain the new one with a merged author list.

Fall 2010: New entries are due 12/10/10. Please append the designation (new Fall 2010) to your new entries.

Spring 2011: New entries are due 5/4/11. Please append the designation (new Spring 2011) to your new entries

Bhatia Lab
: '''[[Molecular Playground/Alginate]]''', David Griffin

: '''[[Molecular Playground/Alginate-Fall2010]]''', Joe White, David Griffin (new Fall 2010)

[http://chamberslab.com/wp/ Chambers Lab]

: '''[[Molecular Playground/Glutamate Receptor]]''', Amanda Hussey, Steve McCarron, Rosie Combs-Bachmann, Mariel Feliciano

[http://openwetware.org/wiki/Chien Chien Lab]

: '''[[Molecular Playground/Hexameric ClpX]]''', Joanne Lau (new Fall 2010)

Forbes Lab

: '''[[Molecular Playground/TRAIL]]''', Charley Swofford

: '''[[Molecular Playground/CheR]]''', Miaomin Zhang (new Spring 2011)

[http://www.biochem.umass.edu/garman/index.html Garman Lab]

: '''[[Molecular Playground/Human Protective Protein Cathepsin A]]''', Yadilette Rivera-Colon

: '''[[Molecular Playground/Human PPCA]]''', Nilima Kolli

[http://people.chem.umass.edu/gieraschlab/ Gierasch Lab]

: '''[[CRABP I ( Cellular Retinoic Acid Binding Protein )|Molecular Playground/CRABP I]]''', Kristine Faye Pobre, Mylene Ferrolino,Mangai Periasamy
:: Best Overall CBI Molecule 2010

[http://people.chem.umass.edu/jhardy/ Hardy Lab]

: '''[[Molecular Playground/Caspase-7 Dynamics]]'''

: '''[[Molecular Playground/Caspase-9 Regulation]]''', Kristen Huber

: '''[[Molecular Playground/Caspase-6 (new)]]''', Elih Velazquez

: '''[[Molecular Playground/Influenza A M2 transmembrane domain]]''', Samantha Nicholls

: '''[[Molecular Playground/Dengue Virus Protease]]''', Muslum Yildiz

Hebert Lab

: '''[[Molecular_Playground/ERMan1]]''', Johan Sunryd

[http://people.biochem.umass.edu/aheuck/aph.html Heuck Lab]

: '''[[Molecular_Playground/Pcr H]]''', Fabian Romano (new Fall 2011)

Kaltashov Lab

: '''[[Molecular Playground/Velaglucerase]]''', Adriana Kita

Knapp lab

:'''[[Molecular Playground/Prolyl Hydroxylase Domain (PHD) Enzyme]]''', Cristina Martin
:: Best CBI Molecule Proteopedia Page 2010

: '''[[Molecular Playground/FIH]]''', Cornelius Taabazuing, Breanne Holmes, John Hangasky

[http://www.chem.umass.edu/~cmartin/ Martin Lab]

: '''[[Molecular Playground/T7 RNA Polymerase (7 mer int)]]''', Ankit Vahia
: '''[[Molecular Playground/T7 RNAP Conformations]]''', Luis E. Ramirez-Tapia (new Fall 2010)

[http://robertsgroup.ecs.umass.edu/ Roberts Lab]

: '''[[Molecular Playground/Taxol]]''', Rohan Patil, Sarah Wilson

: '''[[Molecular Playground/Insulin]]''', Whitney Stoppel

[http://www.umass.edu/rotellogroup/ Rotello Lab]

: '''[[Reverse transcriptase|Molecular Playground/Reverse Transcriptase]]''', Daniel Moyano-Marino

: '''[[Molecular Playground/Pancreatic Lipase]]''', Rui Tang

: '''[[Molecular playground/Chymotrypsin]]''', Brad

: '''[[Molecular Playground/Targeting Peptide]]''', David Solfiell

Schnarr Lab

: '''[[6-deoxyerythronolide_B_synthase_(DEBS)|Molecular Playground/6-Deoxyerythronolide B Synthase]]''', Tsung-Yi Lin, Jon Amoroso

: '''[[Molecular Playground/ACP apo]]''', Gitanjeli Prasad

Thayumanavan Lab

: '''[[Molecular Playground/Lysozime ]]''', Daniella Gonzalez

: '''[[Molecular Playground/Beta-galactosidase]]''', Judy Ventura

: '''[[User:Krishna Reddy Ragupathi|Molecular Playground/Carbonic Anhydrase]]''', Krishna Reddy Raghupathi

: '''[[User:Rami Rajasekhar Reddy|Molecular Playground/Avidin]]''', Rami Rajasekar Reddy

: '''[[Molecular Playground/Biotin binding avidin]]''', Diego Amado

: '''[[User:Jiaming Zhuang|Molecular Playground/MMP12]]''', Jiaming Zhuang

: ''' [[User:Jing Guo|Molecular Playground/Gluconase]]''', Jing Guo

: '''[[Molecular Playground/Glutathione Reductase]]''', Reuben Chacko

Thayumanavan & Vachet Labs

: '''[[Molecular Playground/Trypsin]]''', Gladys Murage

[http://people.chem.umass.edu/thompson/index.html Thompson] & [http://www.chem.umass.edu/~rmweis/weislab/ Weis] Labs

: '''[[Molecular Playground/Bacterial Chemotaxis Receptors]]''', Lynmarie K. Thompson, Shiela M. Jones

: '''[[Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor]]''', Meili Yang

[http://www.chem.umass.edu/~vachet/index.html Vachet Lab]

: '''[[Molecular playground/beta 2 microglobulin]]''', Nick Borotto
:: Best CBI Molecule Jmol scenes 2010

: '''[[Molecular Playground/Myoglobin]]''', Yuping Zhou

:'''[[Molecular Playground/ Copper-Zinc Superoxide Dismutase]]''', Shaynah Browne (NEW FALL 2010)

Other Molecules of interest

: '''[[Molecular Playground/PcrA Helicase]]''', Luis E Ramirez-Tapia, [http://www.chem.umass.edu/~cmartin/ Martin Lab]

Other Laboratories

: '''[[Molecular Playground/YKL-40]]''', Ralph A. Francescone III, [http://www.bio.umass.edu/mcb/faculty/Shao.html Shao Lab]

: '''[[Molecular Playground/BLG|Molecular Playground/β-lactoglobulin]]''', Daniel Seeman, Dubin Lab

: '''[[Molecular Playground/ADAM13]]''', Genevieve Abbruzzese, Alfandari Lab

Instructions:

'''Congratulations to the prize-winning CBI molecules noted above! These also provide great examples to follow. Another prize for best CBI Molecules page and/or scene will be awarded in spring 2011!'''

Choose a molecule that is part of your research project.

1. If you don't already have one, request a Proteopedia account and log in. If you are new to Proteopedia, click Help in the navigation box on the left to get started.

2. Make yourself a sandbox page in which you will develop your CBI Molecule scene and description (Enter "User:your name/sandbox 1" (omit quotes) in the search box, then follow instructions to edit this page. See example [[User:Lynmarie K Thompson/Sandbox 1]]).

3. Follow the format of the sample CBI molecule page [[Molecular Playground/Bacterial Chemotaxis Receptors]]. Easiest way to do this is to copy this page (in editing mode), paste it into your sandbox page, keep the first paragraph about CBI molecules, and then edit to describe and display your molecule. Your goal is to make this an interesting, nontechnical description of the molecule. If multiple people in one group work on the same molecule, you can each make different scenes for the same CBI molecule and each describe them on the same proteopedia page. Talk with each other about your plans so you are not duplicating efforts.

4. Create an attractive scene for your molecule: use the scene authoring tools in the edit mode to create the view you like, then copy the wiki text into your window.

5. Choose a "green scene" on your Proteopedia page to suggest for display at the Molecular Playground and specify a "banner" which will be projected with the molecule. This should be a short, one-line headline for your scene that includes the name of the molecule and what is important about the scene or the molecule. Remember to design this for the general public, including non-scientists. My example is: "Molecular Playground banner: A bacterial chemotaxis receptor protein used by bacteria to "smell" their environment."

6. When you are happy with your sandbox page, make yourself a permanent Proteopedia page, which will be editable by others. Enter "Molecular Playground/your molecule" (omit quotes) in the search box, then follow the instructions to create a new page with this title. Copy the content of your sandbox to this new page.

7. When you have finished the final version of your page and scene, edit this CBI Molecules page to add a listing and link for your molecule, following the "Bacterial chemotaxis receptors" example above. Please list your lab group, with your name in parentheses. That way more than one name can be associated with a Molecular Playground page (if there are several students on the Molecular Playground page, please indicate your scene with your initials). It would be great to link the lab names to web pages too.

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-05-04T13:58:27Z

Shaynah Browne:

{{Template:MP_masthead}}

'''Proposed Article Title: Molecular Playground/Copper-Zinc Superoxide Dismutase'''

Banner: Cu/ Zn Superoxide Dismutase keeps you young

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref name="Culotta">PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond, leading to a destabilized protein structure <ref name="Culotta" />. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Human Cu/ Zn superoxide dismutases (SOD) are homodimer proteins, consisting of two identical monomers, found in the cytoplasm of cells. Each monomer contains <scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>one atom of Copper (Cu), and one atom of Zinc (Zn)</scene>. Each Cu is bound to <scene name='User:Shaynah_Browne/Sandbox_1/Cu_cage/3'>four nitrogen atoms in histidines </scene>and each Zn is bound to four atoms as well. A <scene name='User:Shaynah_Browne/Sandbox_1/Disulfide_bond/2'>disulfide bond </scene>is also located in each monomer. Another interesting feature that contributes to the stability of the protein is the tight <scene name='User:Shaynah_Browne/Sandbox_1/Hydrophobic_surface/2'>hydrophobic surface</scene> between the monomers and “the two halves of the βeta (β)- barrel core” <ref name="Battistoni">PMID: 9488695</ref>.
{{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-05-04T13:54:12Z

Shaynah Browne:

{{Template:MP_masthead}}

'''Proposed Article Title: Molecular Playground/Copper-Zinc Superoxide Dismutase'''

Banner: Cu/ Zn Superoxide Dismutase keeps you young

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref name="Culotta">PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond, leading to a destabilized protein structure <ref name="Culotta" />. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Human Cu/ Zn superoxide dismutases (SOD) are homodimer proteins, consisting of two identical monomers, found in the cytoplasm of cells. Each monomer contains <scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>one atom of Copper (Cu), and one atom of Zinc (Zn)</scene>. Each Cu is bound to <scene name='User:Shaynah_Browne/Sandbox_1/Cu_cage/3'>four nitrogen atoms in histidines </scene>and each Zn is bound to four atoms as well. A <scene name='User:Shaynah_Browne/Sandbox_1/Disulfide_bond/2'>disulfide bond </scene>is also located in each monomer. Another interesting feature that contributes to the stability of the protein is the tight <scene name='User:Shaynah_Browne/Sandbox_1/Hydrophobic_surface/2'>hydrophobic surface</scene> between the monomers and “the two halves of the βeta (β)- barrel core” <ref name="Battistoni">PMID: 00219258 </ref>.
{{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}

==References==
<references />

CBI Molecules

2011-05-02T20:15:13Z

Shaynah Browne:

These are molecules under study by members of the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program].
Many of the molecules we study are featured at the [http://www.molecularplayground.org/ Molecular Playground]. Follow the links below to read nontechnical descriptions in Proteopedia.

UMass CBI Members, add your molecules to the list (which is alphabetical by CBI research mentor); follow the instructions below the list.

It's great to build on a previous entry, but you must leave the earlier one intact and make a copy that you improve and mark as new. Later we will retain the new one with a merged author list.

Fall 2010: New entries are due 12/10/10. Please append the designation (new Fall 2010) to your new entries.

Spring 2011: New entries are due 5/4/11. Please append the designation (new Spring 2011) to your new entries

Bhatia Lab
: '''[[Molecular Playground/Alginate]]''', David Griffin

: '''[[Molecular Playground/Alginate-Fall2010]]''', Joe White, David Griffin (new Fall 2010)

[http://chamberslab.com/wp/ Chambers Lab]

: '''[[Molecular Playground/Glutamate Receptor]]''', Amanda Hussey, Steve McCarron, Rosie Combs-Bachmann, Mariel Feliciano

[http://openwetware.org/wiki/Chien Chien Lab]

: '''[[Molecular Playground/Hexameric ClpX]]''', Joanne Lau (new Fall 2010)

Forbes Lab

: '''[[Molecular Playground/TRAIL]]''', Charley Swofford

[http://www.biochem.umass.edu/garman/index.html Garman Lab]

: '''[[Molecular Playground/Human Protective Protein Cathepsin A]]''', Yadilette Rivera-Colon

: '''[[Molecular Playground/Human PPCA]]''', Nilima Kolli

[http://people.chem.umass.edu/gieraschlab/ Gierasch Lab]

: '''[[CRABP I ( Cellular Retinoic Acid Binding Protein )|Molecular Playground/CRABP I]]''', Kristine Faye Pobre, Mylene Ferrolino,Mangai Periasamy
:: Best Overall CBI Molecule 2010

[http://people.chem.umass.edu/jhardy/ Hardy Lab]

: '''[[Molecular Playground/Caspase-7 Dynamics]]'''

: '''[[Molecular Playground/Caspase-9 Regulation]]''', Kristen Huber

: '''[[Molecular Playground/Caspase-6 (new)]]''', Elih Velazquez

: '''[[Molecular Playground/Influenza A M2 transmembrane domain]]''', Samantha Nicholls

: '''[[Molecular Playground/Dengue Virus Protease]]''', Muslum Yildiz

Hebert Lab

: '''[[Molecular_Playground/ERMan1]]''', Johan Sunryd

[http://people.biochem.umass.edu/aheuck/aph.html Heuck Lab]

: '''[[Molecular_Playground/Pcr H]]''', Fabian Romano

Kaltashov Lab

: '''[[Molecular Playground/Velaglucerase]]''', Adriana Kita

Knapp lab

:'''[[Molecular Playground/Prolyl Hydroxylase Domain (PHD) Enzyme]]''', Cristina Martin
:: Best CBI Molecule Proteopedia Page 2010

: '''[[Molecular Playground/FIH]]''', Cornelius Taabazuing, Breanne Holmes, John Hangasky

[http://www.chem.umass.edu/~cmartin/ Martin Lab]

: '''[[Molecular Playground/T7 RNA Polymerase (7 mer int)]]''', Ankit Vahia
: '''[[Molecular Playground/T7 RNAP Conformations]]''', Luis E. Ramirez-Tapia (new Fall 2010)

[http://robertsgroup.ecs.umass.edu/ Roberts Lab]

: '''[[Molecular Playground/Taxol]]''', Rohan Patil, Sarah Wilson

: '''[[Molecular Playground/Insulin]]''', Whitney Stoppel

[http://www.umass.edu/rotellogroup/ Rotello Lab]

: '''[[Reverse transcriptase|Molecular Playground/Reverse Transcriptase]]''', Daniel Moyano-Marino

: '''[[Molecular Playground/Pancreatic Lipase]]''', Rui Tang

: '''[[Molecular playground/Chymotrypsin]]''', Brad

: '''[[Molecular Playground/Targeting Peptide]]''', David Solfiell

Schnarr Lab

: '''[[6-deoxyerythronolide_B_synthase_(DEBS)|Molecular Playground/6-Deoxyerythronolide B Synthase]]''', Tsung-Yi Lin, Jon Amoroso

: '''[[Molecular Playground/ACP apo]]''', Gitanjeli Prasad

Thayumanavan Lab

: '''[[Molecular Playground/Lysozime ]]''', Daniella Gonzalez

: '''[[Molecular Playground/Beta-galactosidase]]''', Judy Ventura

: '''[[User:Krishna Reddy Ragupathi|Molecular Playground/Carbonic Anhydrase]]''', Krishna Reddy Raghupathi

: '''[[User:Rami Rajasekhar Reddy|Molecular Playground/Avidin]]''', Rami Rajasekar Reddy

: '''[[Molecular Playground/Biotin binding avidin]]''', Diego Amado

: '''[[User:Jiaming Zhuang|Molecular Playground/MMP12]]''', Jiaming Zhuang

: ''' [[User:Jing Guo|Molecular Playground/Gluconase]]''', Jing Guo

: '''[[Molecular Playground/Glutathione Reductase]]''', Reuben Chacko

Thayumanavan & Vachet Labs

: '''[[Molecular Playground/Trypsin]]''', Gladys Murage

[http://people.chem.umass.edu/thompson/index.html Thompson] & [http://www.chem.umass.edu/~rmweis/weislab/ Weis] Labs

: '''[[Molecular Playground/Bacterial Chemotaxis Receptors]]''', Lynmarie K. Thompson, Shiela M. Jones

: '''[[Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor]]''', Meili Yang

[http://www.chem.umass.edu/~vachet/index.html Vachet Lab]

: '''[[Molecular playground/beta 2 microglobulin]]''', Nick Borotto
:: Best CBI Molecule Jmol scenes 2010

: '''[[Molecular Playground/Myoglobin]]''', Yuping Zhou

:'''[[Molecular Playground/ Copper-Zinc Superoxide Dismutase]]''', Shaynah Browne

Other Molecules of interest

: '''[[Molecular Playground/PcrA Helicase]]''', Luis E Ramirez-Tapia, [http://www.chem.umass.edu/~cmartin/ Martin Lab]

Other Laboratories

: '''[[Molecular Playground/YKL-40]]''', Ralph A. Francescone III, [http://www.bio.umass.edu/mcb/faculty/Shao.html Shao Lab]

: '''[[Molecular Playground/BLG|Molecular Playground/β-lactoglobulin]]''', Daniel Seeman, Dubin Lab

: '''[[Molecular Playground/ADAM13]]''', Genevieve Abbruzzese, Alfandari Lab

Instructions:

'''Congratulations to the prize-winning CBI molecules noted above! These also provide great examples to follow. Another prize for best CBI Molecules page and/or scene will be awarded in spring 2011!'''

Choose a molecule that is part of your research project.

1. If you don't already have one, request a Proteopedia account and log in. If you are new to Proteopedia, click Help in the navigation box on the left to get started.

2. Make yourself a sandbox page in which you will develop your CBI Molecule scene and description (Enter "User:your name/sandbox 1" (omit quotes) in the search box, then follow instructions to edit this page. See example [[User:Lynmarie K Thompson/Sandbox 1]]).

3. Follow the format of the sample CBI molecule page [[Molecular Playground/Bacterial Chemotaxis Receptors]]. Easiest way to do this is to copy this page (in editing mode), paste it into your sandbox page, keep the first paragraph about CBI molecules, and then edit to describe and display your molecule. Your goal is to make this an interesting, nontechnical description of the molecule. If multiple people in one group work on the same molecule, you can each make different scenes for the same CBI molecule and each describe them on the same proteopedia page. Talk with each other about your plans so you are not duplicating efforts.

4. Create an attractive scene for your molecule: use the scene authoring tools in the edit mode to create the view you like, then copy the wiki text into your window.

5. Choose a "green scene" on your Proteopedia page to suggest for display at the Molecular Playground and specify a "banner" which will be projected with the molecule. This should be a short, one-line headline for your scene that includes the name of the molecule and what is important about the scene or the molecule. Remember to design this for the general public, including non-scientists. My example is: "Molecular Playground banner: A bacterial chemotaxis receptor protein used by bacteria to "smell" their environment."

6. When you are happy with your sandbox page, make yourself a permanent Proteopedia page, which will be editable by others. Enter "Molecular Playground/your molecule" (omit quotes) in the search box, then follow the instructions to create a new page with this title. Copy the content of your sandbox to this new page.

7. When you have finished the final version of your page and scene, edit this CBI Molecules page to add a listing and link for your molecule, following the "Bacterial chemotaxis receptors" example above. Please list your lab group, with your name in parentheses. That way more than one name can be associated with a Molecular Playground page (if there are several students on the Molecular Playground page, please indicate your scene with your initials). It would be great to link the lab names to web pages too.

User:Shaynah Browne/Sandbox 1

2011-04-14T20:44:05Z

Shaynah Browne: User:Shaynah Browne/Sandbox 1 moved to Molecular Playground/ Copper-Zinc Superoxide Dismutase

#REDIRECT [[Molecular Playground/ Copper-Zinc Superoxide Dismutase]]

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-04-14T20:44:05Z

Shaynah Browne: User:Shaynah Browne/Sandbox 1 moved to Molecular Playground/ Copper-Zinc Superoxide Dismutase

{{Template:MP_masthead}}

'''Proposed Article Title: Molecular Playground/Copper-Zinc Superoxide Dismutase'''

Banner: Cu/ Zn Superoxide Dismutase keeps you young

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref name="Culotta">PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond, leading to a destabilized protein structure <ref name="Culotta" />. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Human Cu/ Zn superoxide dismutases (SOD) are homodimer proteins, consisting of two identical monomers, found in the cytoplasm of cells. Each monomer contains <scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>one atom of Copper (Cu), and one atom of Zinc (Zn)</scene>. Each Cu is bound to <scene name='User:Shaynah_Browne/Sandbox_1/Cu_cage/3'>four nitrogen atoms in histidines </scene>and each Zn is bound to four atoms as well. A <scene name='User:Shaynah_Browne/Sandbox_1/Disulfide_bond/2'>disulfide bond </scene>is also located in each monomer. Another interesting feature that contributes to the stability of the protein is the tight <scene name='User:Shaynah_Browne/Sandbox_1/Hydrophobic_surface/2'>hydrophobic surface</scene> between the monomers and “the two halves of the βeta (β)- barrel core” ( insert reference).
{{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-04-14T20:41:17Z

Shaynah Browne:

{{Template:MP_masthead}}

'''Proposed Article Title: Molecular Playground/Copper-Zinc Superoxide Dismutase'''

Banner: Cu/ Zn Superoxide Dismutase keeps you young

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref name="Culotta">PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond, leading to a destabilized protein structure <ref name="Culotta" />. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Human Cu/ Zn superoxide dismutases (SOD) are homodimer proteins, consisting of two identical monomers, found in the cytoplasm of cells. Each monomer contains <scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>one atom of Copper (Cu), and one atom of Zinc (Zn)</scene>. Each Cu is bound to <scene name='User:Shaynah_Browne/Sandbox_1/Cu_cage/3'>four nitrogen atoms in histidines </scene>and each Zn is bound to four atoms as well. A <scene name='User:Shaynah_Browne/Sandbox_1/Disulfide_bond/2'>disulfide bond </scene>is also located in each monomer. Another interesting feature that contributes to the stability of the protein is the tight <scene name='User:Shaynah_Browne/Sandbox_1/Hydrophobic_surface/2'>hydrophobic surface</scene> between the monomers and “the two halves of the βeta (β)- barrel core” ( insert reference).
{{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-04-14T20:40:30Z

Shaynah Browne:

{{Template:MP_masthead}}

'''Proposed Article Title: Molecular Playground/Copper-Zinc Superoxide Dismutase'''

Banner: Cu/ Zn Superoxide Dismutase keeps you young

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref name="Culotta">PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond, leading to a destabilized protein structure <ref name="Culotta" />. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Human Cu/ Zn superoxide dismutases (SOD) are homodimer proteins, consisting of two identical monomers, found in the cytoplasm of cells. Each monomer contains <scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>one atom of Copper (Cu), and one atom of Zinc (Zn)</scene>. Each Cu is bound to <scene name='User:Shaynah_Browne/Sandbox_1/Cu_cage/3'>four nitrogen atoms in histidines </scene>and each Zn is bound to four atoms as well. A <scene name='User:Shaynah_Browne/Sandbox_1/Disulfide_bond/2'>disulfide bond </scene>is also located in each monomer . Another interesting feature that contributes to the stability of the protein is the tight <scene name='User:Shaynah_Browne/Sandbox_1/Hydrophobic_surface/2'>hydrophobic surface</scene> between the monomers and “the two halves of the βeta (β)- barrel core” ( insert reference).
{{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-04-14T20:39:56Z

Shaynah Browne:

{{Template:MP_masthead}}

'''Proposed Article Title: Molecular Playground/Copper-Zinc Superoxide Dismutase'''

Banner: Cu/ Zn Superoxide Dismutase keeps you young

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref name="Culotta">PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond, leading to a destabilized protein structure <ref name="Culotta" />. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Human Cu/ Zn superoxide dismutases (SOD) are homodimer proteins, consisting of two identical monomers, found in the cytoplasm of cells. Each monomer contains <scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>one atom of Copper (Cu), and one atom of Zinc (Zn)</scene>. Each Cu is bound to <scene name='User:Shaynah_Browne/Sandbox_1/Cu_cage/3'>four nitrogen atoms in histidines </scene>and each Zn is bound to four atoms as well. A <scene name='User:Shaynah_Browne/Sandbox_1/Disulfide_bond/2'>disulfide bond</scene>is also located in each monomer . Another interesting feature that contributes to the stability of the protein is the tight <scene name='User:Shaynah_Browne/Sandbox_1/Hydrophobic_surface/2'>hydrophobic surface</scene> between the monomers and “the two halves of the βeta (β)- barrel core” ( insert reference).
{{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-04-14T20:38:24Z

Shaynah Browne:

{{Template:MP_masthead}}

'''Proposed Article Title: Molecular Playground/Copper-Zinc Superoxide Dismutase'''

Banner: Cu/ Zn Superoxide Dismutase keeps you young

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref name="Culotta">PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond, leading to a destabilized protein structure <ref name="Culotta" />. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Human Cu/ Zn superoxide dismutases (SOD) are homodimer proteins, consisting of two identical monomers, found in the cytoplasm of cells. Each monomer contains <scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>one atom of Copper (Cu), and one atom of Zinc (Zn)</scene>. Each Cu is bound to <scene name='User:Shaynah_Browne/Sandbox_1/Cu_cage/3'>four nitrogen atoms in histidines </scene>and each Zn is bound to four atoms as well. A disulfide bond is also located in each monomer <scene name='User:Shaynah_Browne/Sandbox_1/Disulfide_bond/2'>TextToBeDisplayed</scene> . Another interesting feature that contributes to the stability of the protein is the tight <scene name='User:Shaynah_Browne/Sandbox_1/Hydrophobic_surface/2'>hydrophobic surface</scene> between the monomers and “the two halves of the βeta (β)- barrel core” ( insert reference).
{{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-22T20:01:18Z

Shaynah Browne:

{{Template:MP_masthead}}

'''Proposed Article Title: Molecular Playground/Copper-Zinc Superoxide Dismutase'''

Banner: Cu/ Zn Superoxide Dismutase keeps you young

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref name="Culotta">PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond, leading to a destabilized protein structure <ref name="Culotta" />. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Human Cu/ Zn superoxide dismutases (SOD) are homodimer proteins, consisting of two identical monomers, found in the cytoplasm of cells. Each monomer contains <scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>one atom of Copper (Cu), and one atom of Zinc (Zn)</scene>. Each Cu is bound to <scene name='User:Shaynah_Browne/Sandbox_1/Cu_cage/3'>four nitrogen atoms in histidines </scene>and each Zn is bound to four atoms as well. A disulfide bond is also located in each monomer (highlight and label Cys 57 and Cys 46 and insert reference). Another interesting feature that contributes to the stability of the protein is the tight <scene name='User:Shaynah_Browne/Sandbox_1/Hydrophobic_surface/2'>hydrophobic surface</scene> between the monomers and “the two halves of the βeta (β)- barrel core” ( insert reference).
{{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T21:17:56Z

Shaynah Browne:

{{Template:MP_masthead}}

'''Proposed Article Title: Molecular Playground/Copper-Zinc Superoxide Dismutase'''

Banner: Cu/ Zn Superoxide Dismutase keeps you young

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref name="Culotta">PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond, leading to a destabilized protein structure <ref name="Culotta" />. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Human Cu/ Zn superoxide dismutases (SOD) are homodimer proteins, consisting of two identical monomers, found in the cytoplasm of cells. Each monomer contains <scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>one atom of Copper (Cu), and one atom of Zinc (Zn)</scene>. Each Cu is bound to <scene name='User:Shaynah_Browne/Sandbox_1/Cu_cage/3'>four nitrogen atoms in histidines </scene>and each Zn is bound to four atoms as well ( His 63, His 71, His 80, and Asp 83) add reference. A disulfide bond is also located in each monomer (highlight and label Cys 57 and Cys 46 and insert reference). Another interesting feature that contributes to the stability of the protein is the tight <scene name='User:Shaynah_Browne/Sandbox_1/Hydrophobic_surface/2'>hydrophobic surface</scene> between the monomers and “the two halves of the βeta (β)- barrel core” ( insert reference).
{{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T21:13:36Z

Shaynah Browne:

{{Template:MP_masthead}}

'''Proposed Article Title: Molecular Playground/Copper-Zinc Superoxide Dismutase (SOD)'''

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref name="Culotta">PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond, leading to a destabilized protein structure <ref name="Culotta" />. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Human Cu/ Zn superoxide dismutases (SOD) are homodimer proteins, consisting of two identical monomers, found in the cytoplasm of cells. Each monomer contains <scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>one atom of Copper (Cu), and one atom of Zinc (Zn)</scene>. Each Cu is bound to <scene name='User:Shaynah_Browne/Sandbox_1/Cu_cage/3'>four nitrogen atoms in histidines </scene>and each Zn is bound to four atoms as well ( His 63, His 71, His 80, and Asp 83) add reference. A disulfide bond is also located in each monomer (highlight and label Cys 57 and Cys 46 and insert reference). Another interesting feature that contributes to the stability of the protein is the tight <scene name='User:Shaynah_Browne/Sandbox_1/Hydrophobic_surface/2'>hydrophobic surface</scene> between the monomers and “the two halves of the βeta (β)- barrel core” ( insert reference).
{{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T21:11:58Z

Shaynah Browne:

{{Template:MP_masthead}}

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref name="Culotta">PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond, leading to a destabilized protein structure <ref name="Culotta" />. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Human Cu/ Zn superoxide dismutases (SOD) are homodimer proteins, consisting of two identical monomers, found in the cytoplasm of cells. Each monomer contains <scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>one atom of Copper (Cu), and one atom of Zinc (Zn)</scene>. Each Cu is bound to <scene name='User:Shaynah_Browne/Sandbox_1/Cu_cage/3'>four nitrogen atoms in histidines </scene>and each Zn is bound to four atoms as well ( His 63, His 71, His 80, and Asp 83) add reference. A disulfide bond is also located in each monomer (highlight and label Cys 57 and Cys 46 and insert reference). Another interesting feature that contributes to the stability of the protein is the tight <scene name='User:Shaynah_Browne/Sandbox_1/Hydrophobic_surface/2'>hydrophobic surface</scene> between the monomers and “the two halves of the βeta (β)- barrel core” ( insert reference).
{{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T21:09:19Z

Shaynah Browne:

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref name="Culotta">PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond, leading to a destabilized protein structure <ref name="Culotta" />. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Human Cu/ Zn superoxide dismutases (SOD) are homodimer proteins, consisting of two identical monomers, found in the cytoplasm of cells. Each monomer contains <scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>one atom of Copper (Cu), and one atom of Zinc (Zn)</scene>. Each Cu is bound to <scene name='User:Shaynah_Browne/Sandbox_1/Cu_cage/3'>four nitrogen atoms in histidines </scene>and each Zn is bound to four atoms as well ( His 63, His 71, His 80, and Asp 83) add reference. A disulfide bond is also located in each monomer (highlight and label Cys 57 and Cys 46 and insert reference). Another interesting feature that contributes to the stability of the protein is the tight <scene name='User:Shaynah_Browne/Sandbox_1/Hydrophobic_surface/2'>hydrophobic surface</scene> between the monomers and “the two halves of the βeta (β)- barrel core” ( insert reference).

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T20:58:23Z

Shaynah Browne:

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref name="Culotta">PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond, leading to a destabilized protein structure <ref name="Culotta" />. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Human Cu/ Zn superoxide dismutases (SOD) are homodimer proteins, consisting of two identical monomers, found in the cytoplasm of cells. Each monomer contains <scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>one atom of Copper (Cu), and one atom of Zinc (Zn)</scene>. Each Cu is bound to <scene name='User:Shaynah_Browne/Sandbox_1/Cu_cage/3'>four nitrogen atoms in histidines </scene>and each Zn is bound to four atoms as well ( His 63, His 71, His 80, and Asp 83) add reference. A disulfide bond is also located in each monomer (highlight and label Cys 57 and Cys 46 and insert reference). Another interesting feature that contributes to the stability of the protein is the tight hydrophobic interface between the monomers (highlight hydrophobic interface of the dimer) and “the two halves of the βeta (β)- barrel core” ( insert reference).

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T20:51:34Z

Shaynah Browne:

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref name="Culotta">PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond, leading to a destabilized protein structure <ref name="Culotta" />. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Human Cu/ Zn superoxide dismutases (SOD) are homodimer proteins, consisting of two identical monomers, found in the cytoplasm of cells. Each monomer contains <scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>one atom of Copper (Cu), and one atom of Zinc (Zn)</scene>. Each Cu is bound to <scene name='User:Shaynah_Browne/Sandbox_1/Cu_cage/2'>four nitrogen atoms in histidines </scene>and each Zn is bound to four atoms as well ( His 63, His 71, His 80, and Asp 83) add reference. A disulfide bond is also located in each monomer (highlight and label Cys 57 and Cys 46 and insert reference). Another interesting feature that contributes to the stability of the protein is the tight hydrophobic interface between the monomers (highlight hydrophobic interface of the dimer) and “the two halves of the βeta (β)- barrel core” ( insert reference).

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T20:47:33Z

Shaynah Browne:

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref name="Culotta">PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond, leading to a destabilized protein structure <ref name="Culotta" />. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Human Cu/ Zn superoxide dismutases (SOD) are homodimer proteins, consisting of two identical monomers, found in the cytoplasm of cells. Each monomer contains <scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>one atom of Copper (Cu), and one atom of Zinc (Zn)</scene>. Each Cu is bound to <scene name='User:Shaynah_Browne/Sandbox_1/Cu_cage/1'>four nitrogen atoms in histidines </scene>and each Zn is bound to four atoms as well ( His 63, His 71, His 80, and Asp 83) add reference. A disulfide bond is also located in each monomer (highlight and label Cys 57 and Cys 46 and insert reference). Another interesting feature that contributes to the stability of the protein is the tight hydrophobic interface between the monomers (highlight hydrophobic interface of the dimer) and “the two halves of the βeta (β)- barrel core” ( insert reference).

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T20:13:06Z

Shaynah Browne:

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref name="Culotta">PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond, leading to a destabilized protein structure <ref name="Culotta" />. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Human Cu/ Zn superoxide dismutases (SOD) are homodimer proteins, consisting of two identical monomers, found in the cytoplasm of cells. Each monomer contains <scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>one atom of Copper (Cu), and one atom of Zinc (Zn)</scene>. Each Cu is bound to four nitrogen atoms (show his His 46, 48, 63, 120) and each Zn is bound to four atoms as well ( His 63, His 71, His 80, and Asp 83) add reference. A disulfide bond is also located in each monomer (highlight and label Cys 57 and Cys 46 and insert reference). Another interesting feature that contributes to the stability of the protein is the tight hydrophobic interface between the monomers (highlight hydrophobic interface of the dimer) and “the two halves of the βeta (β)- barrel core” ( insert reference).

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T20:11:20Z

Shaynah Browne:

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref name="Culotta">PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond, leading to a destabilized protein structure <ref name="Culotta" />. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Human Cu/ Zn superoxide dismutases (SOD) are homodimer proteins, consisting of two identical monomers, found in the cytoplasm of cells. Each monomer contains one atom of Copper (Cu), and one atom of Zinc (Zn)<scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>TextToBeDisplayed</scene>. Each Cu is bound to four nitrogen atoms (show his His 46, 48, 63, 120) and each Zn is bound to four atoms as well ( His 63, His 71, His 80, and Asp 83) add reference. A disulfide bond is also located in each monomer (highlight and label Cys 57 and Cys 46 and insert reference). Another interesting feature that contributes to the stability of the protein is the tight hydrophobic interface between the monomers (highlight hydrophobic interface of the dimer) and “the two halves of the βeta (β)- barrel core” ( insert reference).

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T20:09:05Z

Shaynah Browne:

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref name="Culotta">PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond, leading to a destabilized protein structure <ref name="Culotta" />. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Human Cu/ Zn superoxide dismutases (SOD) are homodimer proteins, consisting of two identical monomers, found in the cytoplasm of cells. Each monomer contains one atom of Copper (Cu), and one atom of Zinc (Zn) (highlight Cu and Zn). Each Cu is bound to four nitrogen atoms (show his His 46, 48, 63, 120) and each Zn is bound to four atoms as well ( His 63, His 71, His 80, and Asp 83) add reference. A disulfide bond is also located in each monomer (highlight and label Cys 57 and Cys 46 and insert reference). Another interesting feature that contributes to the stability of the protein is the tight hydrophobic interface between the monomers (highlight hydrophobic interface of the dimer) and “the two halves of the βeta (β)- barrel core” ( insert reference).

<scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>TextToBeDisplayed</scene>

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T20:08:12Z

Shaynah Browne:

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T20:06:29Z

Shaynah Browne:

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T20:05:13Z

Shaynah Browne:

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref name="Culotta">PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond (show reduced disulfide bond reduction), leading to a destabilized protein structure <ref name="Culotta" />. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''
<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>TextToBeDisplayed</scene>

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T20:02:28Z

Shaynah Browne:

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref>PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond (show reduced disulfide bond reduction), leading to a destabilized protein structure <ref>PMID: 16828895</ref>. This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''
<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>TextToBeDisplayed</scene>

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T19:57:29Z

Shaynah Browne:

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes<ref>PMID: 16828895</ref>. One of the reported mutations involves the reduction of the disulfide bond (show reduced disulfide bond reduction), leading to a destabilized protein structure (reference). This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''
<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>TextToBeDisplayed</scene>

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T19:52:26Z

Shaynah Browne:

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis ([[Superoxide Dismutase|ALS]]) and diabetes. (reference). One of the reported mutations involves the reduction of the disulfide bond (show reduced disulfide bond reduction), leading to a destabilized protein structure (reference). This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''
<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>TextToBeDisplayed</scene>

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T19:49:29Z

Shaynah Browne:

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis (ALS) (Wikipedia add reference) and diabetes. (reference). One of the reported mutations involves the reduction of the disulfide bond (show reduced disulfide bond reduction), leading to a destabilized protein structure (reference). This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''
<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>TextToBeDisplayed</scene>

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T19:44:52Z

Shaynah Browne:

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD) is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-) anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis (ALS) (Wikipedia add reference) and diabetes. (reference). One of the reported mutations involves the reduction of the disulfide bond (show reduced disulfide bond reduction), leading to a destabilized protein structure (reference). This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''
<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>TextToBeDisplayed</scene>

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T19:39:51Z

Shaynah Browne:

The important function of Cu/ Zn [[Superoxide Dismutase|superoxide dismutase]] (SOD)is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-), anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis (ALS) (Wikipedia add reference) and diabetes. (reference). One of the reported mutations involves the reduction of the disulfide bond (show reduced disulfide bond reduction), leading to a destabilized protein structure (reference). This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''
<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>TextToBeDisplayed</scene>

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T19:38:46Z

Shaynah Browne:

The important function of Cu/ Zn [[superoxide dismutase]](SOD)is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-), anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis (ALS) (Wikipedia add reference) and diabetes. (reference). One of the reported mutations involves the reduction of the disulfide bond (show reduced disulfide bond reduction), leading to a destabilized protein structure (reference). This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''
<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>TextToBeDisplayed</scene>

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-20T19:34:53Z

Shaynah Browne:

The important function of Cu/ Zn SOD is to detoxify damaging forms of oxygen. It catalyzes the dismutation of superoxide (O2-), anion into molecular oxygen (O2) and hydrogen peroxide (H2O2)<ref>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase in Wikipedia]</ref>. Mutations or disruptions in the protein can exacerbate a number of diseases, such as amyotrophic lateral sclerosis (ALS) (Wikipedia add reference) and diabetes. (reference). One of the reported mutations involves the reduction of the disulfide bond (show reduced disulfide bond reduction), leading to a destabilized protein structure (reference). This mutation is featured in the fatal ALS disease. The motor neurons of individuals are affected, and voluntary muscle control is lost.

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''
<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>TextToBeDisplayed</scene>

==References==
<references />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-13T19:36:34Z

Shaynah Browne:

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''
<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/4'>TextToBeDisplayed</scene>

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-13T19:23:01Z

Shaynah Browne:

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''
<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/3'>TextToBeDisplayed</scene>

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-13T19:11:48Z

Shaynah Browne:

'''Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)'''
<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/1'>TextToBeDisplayed</scene>

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-13T19:10:43Z

Shaynah Browne:

Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/1'>TextToBeDisplayed</scene>

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-13T19:04:53Z

Shaynah Browne:

{{Template:MP_masthead}}
Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)

{{Clear}}
<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<scene name='User:Shaynah_Browne/Sandbox_1/Transparent_surface/1'>TextToBeDisplayed</scene>

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-13T18:47:34Z

Shaynah Browne:

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-13T18:46:19Z

Shaynah Browne:

Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)

{{Template:MP_masthead}}

<Structure load='1cbj' size='400' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-13T18:34:22Z

Shaynah Browne:

Proposed Article Title: Copper Zinc Superoxide Dismutase (SOD)

{{Template:MP_masthead}}

Molecular Playground/ Copper-Zinc Superoxide Dismutase

2011-01-13T18:34:01Z

Shaynah Browne: New page: Proposed Article Title: Copper Zinc Superoxide Dismutase(SOD) {{Template:MP_masthead}}

Proposed Article Title: Copper Zinc Superoxide Dismutase(SOD)

{{Template:MP_masthead}}

User:Shaynah Browne

2011-01-13T18:30:30Z

Shaynah Browne:

I am a chemistry graduate student at the University of Massachusetts, Amherst participating in the Chemistry-Biology Interface Training program (CBI).

*[[User:Shaynah Browne/Sandbox 1]]

Sandbox Copper Zinc Superoxide Dismutase

2010-11-09T18:50:53Z

Shaynah Browne:

Sandbox Copper Zinc Superoxide Dismutase

2010-11-09T18:47:59Z

Shaynah Browne: New page: ==This is a placeholder== This is a placeholder text to help you get started in placing a Jmol applet on your page. At any time, click "Show Preview" at the bottom of this page to see how...

==This is a placeholder==
This is a placeholder text to help you get started in
placing a Jmol applet on your page. At any time, click
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Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load
and display another structure.

{{STRUCTURE_3cin | PDB=3cin | SCENE= }}