2hea: Difference between revisions
New page: left|200px<br /> <applet load="2hea" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hea, resolution 1.8Å" /> '''CONTRIBUTION OF WATE... |
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'''CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY'''<br /> | '''CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2HEA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | 2HEA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=2HEA OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: o-glycosyl]] | [[Category: o-glycosyl]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:31:35 2008'' | ||
Revision as of 18:31, 15 February 2008
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CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY
OverviewOverview
Water molecules frequently occur in the interior of globular proteins. To, elucidate the contribution of buried water molecules to the conformational, stability of a protein, we examined the crystal structures and the, thermodynamic parameters of denaturation of six Ile to Ala/Gly mutant, human lysozymes, in which a cavity is created at each mutation site by the, substitution of a smaller side-chain for a larger one. One or two ordered, water molecules were found in the cavities created in some mutants (I106A, I59A and I59G). The cavity volumes for these three mutants were bigger, than those that remained empty in the other mutants. The stability of the, mutant proteins with the newly introduced water molecules was about 8, kJ/mol higher than that expected from the change in hydrophobic surface, area (DeltaDeltaASAHP) exposed upon denaturation. It was concluded that a, water molecule in a cavity created in the interior of a protein, contributes favorably to the stability.
DiseaseDisease
Known diseases associated with this structure: Amyloidosis, renal OMIM:[153450], Microphthalmia, syndromic 1 OMIM:[309800]
About this StructureAbout this Structure
2HEA is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
ReferenceReference
Contribution of water molecules in the interior of a protein to the conformational stability., Takano K, Funahashi J, Yamagata Y, Fujii S, Yutani K, J Mol Biol. 1997 Nov 21;274(1):132-42. PMID:9398521
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