1uue: Difference between revisions

Revision as of 06:28, 29 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:1uue.png

Template:STRUCTURE 1uue

A-SPECTRIN SH3 DOMAIN (V44T, D48G MUTANT)A-SPECTRIN SH3 DOMAIN (V44T, D48G MUTANT)

Template:ABSTRACT PUBMED 14978284

About this StructureAbout this Structure

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

ReferenceReference

Solvation in protein folding analysis: combination of theoretical and experimental approaches., Fernandez-Escamilla AM, Cheung MS, Vega MC, Wilmanns M, Onuchic JN, Serrano L, Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):2834-9. Epub 2004 Feb 20. PMID:14978284

Page seeded by OCA on Tue Jul 29 06:28:30 2008

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

OCA

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-'''A-SPECTRIN SH3 DOMAIN (V44T, D48G MUTANT)'''
+===A-SPECTRIN SH3 DOMAIN (V44T, D48G MUTANT)===
-==Overview==
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-An effort to combine theoretical analyses and protein engineering methods has been made to probe the folding mechanism of SH3 by using Energy Landscape Theory and a phi-value analysis. Particular emphasis was given to core residues and the effect of desolvation during the folding event by replacing the core valines with isosteric threonines. These mutations have the advantage of keeping the core structurally invariant while affecting core stability relative to the unfolded state. Although the valines that form the core appear spatially invariant, the folding kinetics of their threonine mutants varies, indicating their different extent of solvation in the transition-state ensemble. Theoretical studies predicted the distribution of folding kinetics of threonine mutants without previous knowledge of the measured rates. This initial success encourages further investigations of the molecular details behind these macroscopic phenomena and of the role of solvation in the folding mechanism.
+The line below this paragraph, {{ABSTRACT_PUBMED_14978284}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14978284 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14978284}}
 ==About this Structure==
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 [[Category: Sh3-domain]]
 [[Category: Spectrin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:42:19 2008''
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