1tuc: Difference between revisions

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[[Image:1tuc.gif|left|200px]]
{{Seed}}
[[Image:1tuc.png|left|200px]]


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{{STRUCTURE_1tuc|  PDB=1tuc  |  SCENE=  }}  
{{STRUCTURE_1tuc|  PDB=1tuc  |  SCENE=  }}  


'''ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT S19-P20'''
===ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT S19-P20===




==Overview==
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We have analyzed the structure, stability and folding kinetics of circularly permuted forms of alpha-spectrin SH3 domain. All the possible permutations involving the disruption of the covalent linkage between two beta-strands forming a beta-hairpin have been done. The different proteins constructed here fold to a native conformation similar to that of wild-type protein, as demonstrated by nuclear magnetic resonance and circular dichroism. Although all the mutants have similar stabilities (they are 1 to 2 kcal mol-1 less stable than the wild-type) their rate constants for folding and unfolding are quite different. Protein engineering, in combination with kinetics indicates that the folding pathway has been changed in the circularly permuted proteins. We conclude that neither the order of secondary structure elements, nor the preservation of any of the beta-hairpins present in this domain, is crucial for the ability of the polypeptide to fold, but they influence the folding and unfolding kinetics and could determine its folding pathway.
The line below this paragraph, {{ABSTRACT_PUBMED_7723022}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 7723022 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7723022}}


==About this Structure==
==About this Structure==
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[[Category: Repeat]]
[[Category: Repeat]]
[[Category: Sh3 domain]]
[[Category: Sh3 domain]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:22:30 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:30:09 2008''

Revision as of 00:30, 29 July 2008

File:1tuc.png

Template:STRUCTURE 1tuc

ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT S19-P20

Template:ABSTRACT PUBMED 7723022

About this Structure

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

Reference

The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics., Viguera AR, Blanco FJ, Serrano L, J Mol Biol. 1995 Apr 7;247(4):670-81. PMID:7723022

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