2h70: Difference between revisions

Revision as of 19:25, 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:2h70.png

Template:STRUCTURE 2h70

Crystal Structure of Thioredoxin Mutant D9E in Hexagonal (p61) Space GroupCrystal Structure of Thioredoxin Mutant D9E in Hexagonal (p61) Space Group

Template:ABSTRACT PUBMED 16100262

About this StructureAbout this Structure

2H70 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

A stability pattern of protein hydrophobic mutations that reflects evolutionary structural optimization., Godoy-Ruiz R, Perez-Jimenez R, Ibarra-Molero B, Sanchez-Ruiz JM, Biophys J. 2005 Nov;89(5):3320-31. Epub 2005 Aug 12. PMID:16100262

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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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-'''Crystal Structure of Thioredoxin Mutant D9E in Hexagonal (p61) Space Group'''
+===Crystal Structure of Thioredoxin Mutant D9E in Hexagonal (p61) Space Group===
-==Overview==
+<!--
-We have determined the effect of mutations involving isoleucine and valine (i.e., mutations I--&gt;V and V--&gt;I) on the stability of Escherichia coli thioredoxin. Despite the similarity in chemical structure (V and I differ only in a methyl group), we find that many environments are optimized to a significant extent for either V or I. We find, furthermore, that a plot of effect of hydrophobic mutations on stability versus packing density shows a strikingly simple pattern that clearly reflects evolutionary structural optimization. The existence of such patterns suggests the possibility of rationalizing (and perhaps even predicting) mutation effects on protein stability on the basis of evolutionary models. By "evolutionary model" we specifically refer in this context to a model for mutation effects on stability in which certain physical features of the mutated residue environments are evaluated from an assumption regarding how such environments have been selected during protein evolution (as opposed to a purely "physical model" in which those features would be derived from some kind of energetics analysis of the protein structural characteristics). To illustrate this novel approach and provide general guidelines for its application, we develop here a simple evolutionary model that successfully explains the effect of the I&lt;--&gt;V mutations on thioredoxin stability.
+The line below this paragraph, {{ABSTRACT_PUBMED_16100262}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16100262}}
 ==About this Structure==
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 [[Category: Alpha beta]]
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