1e6h

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[[Image:1e6h.jpg|left|200px]]
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{{Seed}}
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[[Image:1e6h.png|left|200px]]
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{{STRUCTURE_1e6h| PDB=1e6h | SCENE= }}
{{STRUCTURE_1e6h| PDB=1e6h | SCENE= }}
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'''A-SPECTRIN SH3 DOMAIN A11V, M25I, V44I, V58L MUTANTS'''
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===A-SPECTRIN SH3 DOMAIN A11V, M25I, V44I, V58L MUTANTS===
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==Overview==
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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--&gt;Val) leads to deceleration in unfolding and increased stability (up to 2 kcal x mol(-1)). Several of these Ile--&gt;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.
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The line below this paragraph, {{ABSTRACT_PUBMED_12006985}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 12006985 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12006985}}
==About this Structure==
==About this Structure==
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[[Category: Cytoskeleton]]
[[Category: Cytoskeleton]]
[[Category: Sh3-domain]]
[[Category: Sh3-domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:43:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:13:56 2008''

Revision as of 21:14, 30 June 2008

Template:STRUCTURE 1e6h

A-SPECTRIN SH3 DOMAIN A11V, M25I, V44I, V58L MUTANTS

Template:ABSTRACT PUBMED 12006985

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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