1e6h
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(New page: 200px<br /><applet load="1e6h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e6h, resolution 2.01Å" /> '''A-SPECTRIN SH3 DOMAI...)
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Revision as of 11:40, 20 November 2007
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A-SPECTRIN SH3 DOMAIN A11V, M25I, V44I, V58L MUTANTS
Overview
We have designed de novo 13 divergent spectrin SH3 core sequences to, determine their folding properties. Kinetic analysis of the variants with, stability similar to that of the wild type protein shows accelerated, unfolding and refolding rates compatible with a preferential stabilization, of the transition state. This is most likely caused by conformational, strain in the native state, as deletion of a methyl group (Ile-->Val), leads to deceleration in unfolding and increased stability (up to 2 kcal x, mol(-1)). Several of these Ile-->Val mutants have negative phi(-U) values, indicating that some noncanonical phi(-U) values might result from, conformational strain. Thus, producing a stable protein does not, necessarily mean that the design process has been entirely successful., Strained interactions could have been introduced, and a reduction in the, buried volume could result in a large increase in stability and a, reduction in unfolding rates.
About this Structure
1E6H is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Conformational strain in the hydrophobic core and its implications for protein folding and design., Ventura S, Vega MC, Lacroix E, Angrand I, Spagnolo L, Serrano L, Nat Struct Biol. 2002 Jun;9(6):485-93. PMID:12006985
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