Inherent flexibility determines the transition mechanisms of the EF-hands of calmodulin

We explore how inherent flexibility of a protein molecule influences the mechanism controlling allosteric transitions by using a variational model inspired from work in protein folding. The striking differences in the predicted transition mechanism for the opening of the two domains of calmodulin (C...

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Bibliographic Details

Published in:	Proceedings of the National Academy of Sciences - PNAS Vol. 106; no. 7; p. 2104
Main Authors:	Tripathi, Swarnendu, Portman, John J
Format:	Journal Article
Language:	English
Published:	United States 17.02.2009
Subjects:	Allosteric Site Amino Acid Motifs Calcium - metabolism Calmodulin - chemistry EF Hand Motifs - genetics Humans Kinetics Models, Molecular Models, Statistical Molecular Conformation Pliability Protein Conformation Protein Folding Protein Structure, Secondary Protein Structure, Tertiary
ISSN:	1091-6490, 1091-6490
Online Access:	Get more information
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