2b6x: Difference between revisions

Revision as of 18:23, 28 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:2b6x.jpg

Template:STRUCTURE 2b6x

T4 Lysozyme mutant L99A at 200 MPaT4 Lysozyme mutant L99A at 200 MPa

Template:ABSTRACT PUBMED 16269539

About this StructureAbout this Structure

2B6X is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

ReferenceReference

Cooperative water filling of a nonpolar protein cavity observed by high-pressure crystallography and simulation., Collins MD, Hummer G, Quillin ML, Matthews BW, Gruner SM, Proc Natl Acad Sci U S A. 2005 Nov 15;102(46):16668-71. Epub 2005 Nov 3. PMID:16269539

Page seeded by OCA on Mon Jul 28 18:23:46 2008

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

OCA

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-'''T4 Lysozyme mutant L99A at 200 MPa'''
+===T4 Lysozyme mutant L99A at 200 MPa===
-==Overview==
+<!--
-Formation of a water-expelling nonpolar core is the paradigm of protein folding and stability. Although experiment largely confirms this picture, water buried in "hydrophobic" cavities is required for the function of some proteins. Hydration of the protein core has also been suggested as the mechanism of pressure-induced unfolding. We therefore are led to ask whether even the most nonpolar protein core is truly hydrophobic (i.e., water-repelling). To answer this question we probed the hydration of an approximately 160-A(3), highly hydrophobic cavity created by mutation in T4 lysozyme by using high-pressure crystallography and molecular dynamics simulation. We show that application of modest pressure causes approximately four water molecules to enter the cavity while the protein itself remains essentially unchanged. The highly cooperative filling is primarily due to a small change in bulk water activity, which implies that changing solvent conditions or, equivalently, cavity polarity can dramatically affect interior hydration of proteins and thereby influence both protein activity and folding.
+The line below this paragraph, {{ABSTRACT_PUBMED_16269539}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16269539 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16269539}}
 ==About this Structure==
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 [[Category: High pressure]]
 [[Category: T4 lysozyme]]
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