1gxv: Difference between revisions

Revision as of 06:17, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1gxv.png

Template:STRUCTURE 1gxv

SOLUTION STRUCTURE OF LYSOZYME AT LOW AND HIGH PRESSURESOLUTION STRUCTURE OF LYSOZYME AT LOW AND HIGH PRESSURE

Template:ABSTRACT PUBMED 12654268

About this StructureAbout this Structure

1GXV is a Single protein structure of sequence from Gallus gallus. Full experimental information is available from OCA.

ReferenceReference

Pressure-dependent changes in the solution structure of hen egg-white lysozyme., Refaee M, Tezuka T, Akasaka K, Williamson MP, J Mol Biol. 2003 Apr 4;327(4):857-65. PMID:12654268

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''SOLUTION STRUCTURE OF LYSOZYME AT LOW AND HIGH PRESSURE'''
+===SOLUTION STRUCTURE OF LYSOZYME AT LOW AND HIGH PRESSURE===
-==Overview==
+<!--
-The "rules" governing protein structure and stability are still poorly understood. Important clues have come from proteins that operate under extreme conditions, because these clarify the physical constraints on proteins. One obvious extreme is pressure, but so far little is known of the behavior of proteins under pressure, largely for technical reasons. We have therefore developed new methodology for calculating structure change in solution with pressure, using NMR chemical shift changes, and we report the change in structure of lysozyme on going from 30 bar to 2000 bar, this being the first solution structure of a globular protein under pressure. The alpha-helical domain is compressed by approximately 1%, due to tighter packing between helices. The interdomain region is also compressed. By contrast, the beta-sheet domain displays very little overall compression, but undergoes more structural distortion than the alpha-domain. The largest volume changes tend to occur close to hydrated cavities. Because isothermal compressibility is related to volume fluctuation, this suggests that buried water molecules play an important role in conformational fluctuation at normal pressures, and are implicated as the nucleation sites for structural changes leading to pressure denaturation or channel opening.
+The line below this paragraph, {{ABSTRACT_PUBMED_12654268}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12654268 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12654268}}
 ==About this Structure==
-GXV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GXV OCA].
+GXV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GXV OCA].
 ==Reference==
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 [[Category: Saccharide degradation,glycosidase]]
 [[Category: Signal]]
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