1yl0: Difference between revisions
New page: left|200px<br /><applet load="1yl0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yl0, resolution 1.9Å" /> '''Effect of alcohols on... |
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[[Image:1yl0.gif|left|200px]]<br /><applet load="1yl0" size=" | [[Image:1yl0.gif|left|200px]]<br /><applet load="1yl0" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1yl0, resolution 1.9Å" /> | caption="1yl0, resolution 1.9Å" /> | ||
'''Effect of alcohols on protein hydration'''<br /> | '''Effect of alcohols on protein hydration'''<br /> | ||
==Overview== | ==Overview== | ||
Organic solvents are known to bring about dehydration of proteins, the | Organic solvents are known to bring about dehydration of proteins, the molecular basis of which has remained uncharacterized. The dehydration effect in many cases leads to eventual unfolding of proteins through the macroscopic solvent effect. In some cases, the organic solvent molecules also bind to protein surfaces, thereby forcing local unfolding. The X-ray structure of hen egg-white lysozyme co-crystallized in the presence of alcohols with varying hydrophobicities has been studied. It was noticed that although the alcohols have very little effect on the conformation of the overall protein structure, they profoundly affect protein hydration and disorder of the bound waters. Systematic analysis of the water structure around the lysozyme molecule suggests that an increasing order of hydrophobicity of alcohols is directly proportional to the higher number of weakly bound waters in the protein. As anticipated, the water molecules in the native structure with high temperature factors (>/=40 A(2)) attain higher disorder in the presence of alcohols. It is believed that the disorder induced in the water molecules is a direct consequence of alcohol binding. | ||
==About this Structure== | ==About this Structure== | ||
1YL0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with NA, CL and IPA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http:// | 1YL0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=IPA:'>IPA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YL0 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Deshpande, A.]] | [[Category: Deshpande, A.]] | ||
[[Category: Mande, S | [[Category: Mande, S C.]] | ||
[[Category: Nimsadkar, S.]] | [[Category: Nimsadkar, S.]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: water structure]] | [[Category: water structure]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:06:23 2008'' | ||
Revision as of 17:06, 21 February 2008
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Effect of alcohols on protein hydration
OverviewOverview
Organic solvents are known to bring about dehydration of proteins, the molecular basis of which has remained uncharacterized. The dehydration effect in many cases leads to eventual unfolding of proteins through the macroscopic solvent effect. In some cases, the organic solvent molecules also bind to protein surfaces, thereby forcing local unfolding. The X-ray structure of hen egg-white lysozyme co-crystallized in the presence of alcohols with varying hydrophobicities has been studied. It was noticed that although the alcohols have very little effect on the conformation of the overall protein structure, they profoundly affect protein hydration and disorder of the bound waters. Systematic analysis of the water structure around the lysozyme molecule suggests that an increasing order of hydrophobicity of alcohols is directly proportional to the higher number of weakly bound waters in the protein. As anticipated, the water molecules in the native structure with high temperature factors (>/=40 A(2)) attain higher disorder in the presence of alcohols. It is believed that the disorder induced in the water molecules is a direct consequence of alcohol binding.
About this StructureAbout this Structure
1YL0 is a Single protein structure of sequence from Gallus gallus with , and as ligands. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
ReferenceReference
Effect of alcohols on protein hydration: crystallographic analysis of hen egg-white lysozyme in the presence of alcohols., Deshpande A, Nimsadkar S, Mande SC, Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):1005-8. Epub 2005, Jun 24. PMID:15983424
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