https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Raisa+Kantaev 2026-09-18T23:28:29Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=File:1HLPfromPymol0001.png&diff=1640003 2012-12-25T16:00:33Z

<p>Raisa Kantaev: </p> <hr /> <div></div>

Raisa Kantaev https://proteopedia.org/index.php?title=Halophilic_malate_dehydrogenase&diff=1639935 2012-12-24T19:50:26Z

<p>Raisa Kantaev: </p> <hr /> <div>== ''Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium'' ==<br /> &lt;StructureSection load='1HLP' size='500' side='center' caption='3D Structure of halophilic malate dehydrogenase ' scene=''&gt;<br /> <br /> <br /> == '''Scheme''' ==<br /> <br /> The high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui [[http://www.highbeam.com/doc/1G1-16845034.html]] was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic residues distributed on the enzyme &lt;scene name='WISPSF201208/Cationic_and_anionic_residues/1'&gt;surface&lt;/scene&gt; and more salt bridges present in hMDH compared with its nonhalophilic counterparts. Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH<br /> <br /> <br /> <br /> <br /> <br /> '''edited by Ariel Zinger and Raisa Kantaev'''</div>

Raisa Kantaev https://proteopedia.org/index.php?title=Halophilic_malate_dehydrogenase&diff=1639934 2012-12-24T19:42:31Z

<p>Raisa Kantaev: </p> <hr /> <div>== ''Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium'' ==<br /> &lt;StructureSection load='1HLP' size='500' side='center' caption='3D Structure of halophilic malate dehydrogenase ' scene=''&gt;<br /> <br /> <br /> == '''Scheme''' ==<br /> <br /> The high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui [[http://www.highbeam.com/doc/1G1-16845034.html]] was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic residues distributed on the enzyme &lt;scene name='WISPSF201208/Cationic_and_anionic_residues/1'&gt;'surface'&lt;/scene&gt; and more salt bridges present in hMDH compared with its nonhalophilic counterparts. Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH</div>

Raisa Kantaev https://proteopedia.org/index.php?title=Halophilic_malate_dehydrogenase&diff=1639933 2012-12-24T19:37:58Z

<p>Raisa Kantaev: </p> <hr /> <div>== ''Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium'' ==<br /> &lt;StructureSection load='1HLP' size='500' side='center' caption='3D Structure of halophilic malate dehydrogenase ' scene=''&gt;<br /> <br /> <br /> == '''Scheme''' ==<br /> <br /> The high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui [[http://www.highbeam.com/doc/1G1-16845034.html]] was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic residues distributed on the enzyme &lt;scene name='WISPSF201208/Cationic_and_anionic_residues/1'&gt;surface&lt;/scene&gt; and more salt bridges present in hMDH compared with its nonhalophilic counterparts. Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH</div>

Raisa Kantaev https://proteopedia.org/index.php?title=Halophilic_malate_dehydrogenase&diff=1639932 2012-12-24T19:36:43Z

<p>Raisa Kantaev: </p> <hr /> <div>== ''Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium'' ==<br /> &lt;StructureSection load='1HLP' size='500' side='center' caption='3D Structure of halophilic malate dehydrogenase ' scene=''&gt;<br /> <br /> <br /> == '''Scheme''' ==<br /> &lt;scene name='WISPSF201208/Cationic_and_anionic_residues/1'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> The high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui [[http://www.highbeam.com/doc/1G1-16845034.html]] was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic residues distributed on the enzyme surface and more salt bridges present in hMDH compared with its nonhalophilic counterparts. Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH</div>

Raisa Kantaev https://proteopedia.org/index.php?title=Halophilic_malate_dehydrogenase&diff=1639931 2012-12-24T19:36:10Z

<p>Raisa Kantaev: </p> <hr /> <div>== ''Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium'' ==<br /> &lt;StructureSection load='1HLP' size='500' side='center' caption='3D Structure of halophilic malate dehydrogenase ' scene='WISPSF201208/Cationic_and_anionic_residues/1'&gt;<br /> <br /> <br /> == '''Scheme''' ==<br /> <br /> The high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui [[http://www.highbeam.com/doc/1G1-16845034.html]] was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic residues distributed on the enzyme surface and more salt bridges present in hMDH compared with its nonhalophilic counterparts. Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH</div>

Raisa Kantaev https://proteopedia.org/index.php?title=Halophilic_malate_dehydrogenase&diff=1639930 2012-12-24T19:35:24Z

<p>Raisa Kantaev: </p> <hr /> <div>== ''Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium'' ==<br /> &lt;StructureSection load='1HLP' size='500' side='center' caption='3D Structure of halophilic malate dehydrogenase ' scene='WISPSF201208/Cationic_and_anionic_residues/1'<br /> <br /> == '''Scheme''' ==<br /> <br /> The &lt;scene name='WISPSF201208/Cationic_and_anionic_residues/1'&gt;TextToBeDisplayed&lt;/scene&gt;high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui [[http://www.highbeam.com/doc/1G1-16845034.html]] was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic residues distributed on the enzyme surface and more salt bridges present in hMDH compared with its nonhalophilic counterparts. Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH</div>

Raisa Kantaev https://proteopedia.org/index.php?title=Halophilic_malate_dehydrogenase&diff=1639929 2012-12-24T19:35:11Z

<p>Raisa Kantaev: </p> <hr /> <div>== ''Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium'' ==<br /> &lt;StructureSection load='1HLP' size='500' side='center' caption='3D Structure of halophilic malate dehydrogenase ' scene='WISPSF201208/Cationic_and_anionic_residues/1' /&gt;<br /> <br /> == '''Scheme''' ==<br /> <br /> The &lt;scene name='WISPSF201208/Cationic_and_anionic_residues/1'&gt;TextToBeDisplayed&lt;/scene&gt;high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui [[http://www.highbeam.com/doc/1G1-16845034.html]] was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic residues distributed on the enzyme surface and more salt bridges present in hMDH compared with its nonhalophilic counterparts. Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH</div>

Raisa Kantaev https://proteopedia.org/index.php?title=Halophilic_malate_dehydrogenase&diff=1639928 2012-12-24T19:34:09Z

<p>Raisa Kantaev: </p> <hr /> <div>== ''Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium'' ==<br /> &lt;StructureSection load='1HLP' size='500' side='center' caption='3D Structure of halophilic malate dehydrogenase ' scene='Insert optional scene name here' /&gt;<br /> <br /> == '''Scheme''' ==<br /> <br /> The &lt;scene name='WISPSF201208/Cationic_and_anionic_residues/1'&gt;TextToBeDisplayed&lt;/scene&gt;high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui [[http://www.highbeam.com/doc/1G1-16845034.html]] was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic residues distributed on the enzyme surface and more salt bridges present in hMDH compared with its nonhalophilic counterparts. Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH</div>

Raisa Kantaev https://proteopedia.org/index.php?title=Halophilic_malate_dehydrogenase&diff=1639927 2012-12-24T19:31:22Z

<p>Raisa Kantaev: </p> <hr /> <div>== ''Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium'' ==<br /> &lt;StructureSection load='1HLP' size='500' side='center' caption='3D Structure of halophilic malate dehydrogenase ' &lt;scene name='WISPSF201208/Cationic_and_anionic_residues/1'&gt;Great&lt;/scene&gt;<br /> <br /> == '''Scheme''' ==<br /> <br /> The high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui [[http://www.highbeam.com/doc/1G1-16845034.html]] was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic residues distributed on the enzyme surface and more salt bridges present in hMDH compared with its nonhalophilic counterparts. Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH</div>

Raisa Kantaev https://proteopedia.org/index.php?title=Halophilic_malate_dehydrogenase&diff=1639926 2012-12-24T19:29:40Z

<p>Raisa Kantaev: </p> <hr /> <div>== ''Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium'' ==<br /> &lt;StructureSection load='1HLP' size='500' side='center' caption='3D Structure of halophilic malate dehydrogenase ' 'scene name='WISPSF201208/Cationic_and_anionic_residues/1'&gt;TextToBeDisplayed&lt;/scene&gt;'<br /> <br /> == '''Scheme''' ==<br /> <br /> The high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui [[http://www.highbeam.com/doc/1G1-16845034.html]] was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic residues distributed on the enzyme surface and more salt bridges present in hMDH compared with its nonhalophilic counterparts. Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH</div>

Raisa Kantaev https://proteopedia.org/index.php?title=Halophilic_malate_dehydrogenase&diff=1639925 2012-12-24T19:28:45Z

<p>Raisa Kantaev: </p> <hr /> <div>== ''Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium'' ==<br /> &lt;StructureSection load='1HLP' size='500' side='center' caption='3D Structure of halophilic malate dehydrogenase ' scene='&lt;scene name='WISPSF201208/Cationic_and_anionic_residues/1'&gt;TextToBeDisplayed&lt;/scene&gt;'&gt;<br /> <br /> == '''Scheme''' ==<br /> <br /> The high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui [[http://www.highbeam.com/doc/1G1-16845034.html]] was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic residues distributed on the enzyme surface and more salt bridges present in hMDH compared with its nonhalophilic counterparts. Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH</div>

Raisa Kantaev https://proteopedia.org/index.php?title=Halophilic_malate_dehydrogenase&diff=1639924 2012-12-24T19:26:21Z

<p>Raisa Kantaev: </p> <hr /> <div>== ''Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium'' ==<br /> &lt;StructureSection load='1HLP' size='500' side='center' caption='3D Structure of halophilic malate dehydrogenase ' scene='Copy and paste the following line where you want the scene link to appear (scroll down if needed) and edit the TextToBeDisplayed:<br /> <br /> &lt;scene name='WISPSF201208/Cationic_and_anionic_residues/1'&gt;TextToBeDisplayed&lt;/scene&gt;'&gt;<br /> <br /> == '''Scheme''' ==<br /> <br /> The high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui [[http://www.highbeam.com/doc/1G1-16845034.html]] was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic residues distributed on the enzyme surface and more salt bridges present in hMDH compared with its nonhalophilic counterparts. Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH</div>

Raisa Kantaev https://proteopedia.org/index.php?title=Halophilic_malate_dehydrogenase&diff=1639923 2012-12-24T19:00:00Z

<p>Raisa Kantaev: </p> <hr /> <div>== ''Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium'' ==<br /> &lt;StructureSection load='1HLP' size='500' side='center' caption='3D Structure of halophilic malate dehydrogenase ' scene=''&gt;<br /> <br /> == '''Scheme''' ==<br /> Ь<br /> The high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui [[http://www.highbeam.com/doc/1G1-16845034.html]] was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic residues distributed on the enzyme surface and more salt bridges present in hMDH compared with its nonhalophilic counterparts. Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH</div>

Raisa Kantaev https://proteopedia.org/index.php?title=Halophilic_malate_dehydrogenase&diff=1639922 2012-12-24T18:52:26Z

<p>Raisa Kantaev: </p> <hr /> <div>== Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium ==<br /> &lt;StructureSection load='1HLP' size='500' side='center' caption='3D Structure of halophilic malate dehydrogenase)' scene=''&gt;<br /> <br /> == Scheme ==<br /> <br /> The high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui [[http://www.highbeam.com/doc/1G1-16845034.html]] was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic residues distributed on the enzyme surface and more salt bridges present in hMDH compared with its nonhalophilic counterparts. Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH</div>

Raisa Kantaev https://proteopedia.org/index.php?title=Halophilic_malate_dehydrogenase&diff=1639921 2012-12-24T18:50:35Z

<p>Raisa Kantaev: </p> <hr /> <div>== Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium ==<br /> &lt;StructureSection load='1HLP' size='500' side='center' caption='3D Structure of halophilic malate dehydrogenase)' scene=''&gt;<br /> <br /> == Scheme ==<br /> <br /> The high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui [[http://www.highbeam.com/doc/1G1-16845034.html]] was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic residues distributed on the enzyme surface and more salt bridges present in hMDH compared with its nonhalophilic counterparts. Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH<br /> <br /> &lt;/StructureSection&gt;<br /> &lt;Structure load='<br /> ----<br /> Insert PDB code or filename here' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;</div>

Raisa Kantaev https://proteopedia.org/index.php?title=Halophilic_malate_dehydrogenase&diff=1639920 2012-12-24T18:49:38Z

<p>Raisa Kantaev: </p> <hr /> <div>== Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium ==<br /> &lt;StructureSection load='1HLP' size='500' side='center' caption='3D Structure of halophilic malate dehydrogenase (PDB entry [[1hlp]])' scene=''&gt;<br /> <br /> <br /> == Scheme ==<br /> The high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui [[http://www.highbeam.com/doc/1G1-16845034.html]] was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic residues distributed on the enzyme surface and more salt bridges present in hMDH compared with its nonhalophilic counterparts. Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH<br /> <br /> &lt;/StructureSection&gt;<br /> &lt;Structure load='<br /> ----<br /> Insert PDB code or filename here' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;</div>

Raisa Kantaev https://proteopedia.org/index.php?title=Halophilic_malate_dehydrogenase&diff=1639919 2012-12-24T18:48:36Z

<p>Raisa Kantaev: </p> <hr /> <div>== Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium ==<br /> &lt;StructureSection load='1HLP' size='500' side='center' caption='3D Structure of halophilic malate dehydrogenase (PDB entry [[1hlp]])' scene=''&gt;<br /> Anything in this section will appear adjacent to the 3D structure and will be scrollable.<br /> <br /> == Scheme ==<br /> The high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui [[http://www.highbeam.com/doc/1G1-16845034.html]] was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic residues distributed on the enzyme surface and more salt bridges present in hMDH compared with its nonhalophilic counterparts. Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH<br /> <br /> &lt;/StructureSection&gt;<br /> &lt;Structure load='<br /> ----<br /> Insert PDB code or filename here' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;</div>

Raisa Kantaev https://proteopedia.org/index.php?title=Halophilic_malate_dehydrogenase&diff=1639918 2012-12-24T18:47:00Z

<p>Raisa Kantaev: </p> <hr /> <div>== Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium ==<br /> &lt;StructureSection load='1HLP' size='500' side='center' caption='3D Structure of halophilic malate dehydrogenase (PDB entry [[1hlp]])' scene=''&gt;<br /> Anything in this section will appear adjacent to the 3D structure and will be scrollable.<br /> <br /> == Structure ==<br /> [[http://www.highbeam.com/doc/1G1-16845034.html]]<br /> &lt;/StructureSection&gt;<br /> &lt;Structure load='<br /> ----<br /> Insert PDB code or filename here' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;</div>

Raisa Kantaev https://proteopedia.org/index.php?title=Halophilic_malate_dehydrogenase&diff=1639917 2012-12-24T18:46:10Z

<p>Raisa Kantaev: </p> <hr /> <div>== Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium ==<br /> &lt;StructureSection load='1HLP' size='500' side='center' caption='3D Structure of halophilic malate dehydrogenase (PDB entry [[1hlp]])' scene=''&gt;<br /> Anything in this section will appear adjacent to the 3D structure and will be scrollable.<br /> <br /> == Structure ==<br /> <br /> &lt;/StructureSection&gt;<br /> &lt;Structure load='<br /> ----<br /> Insert PDB code or filename here' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;</div>

Raisa Kantaev