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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Vydané v:	Proceedings of the National Academy of Sciences - PNAS Ročník 106; číslo 7; s. 2104
Hlavní autori:	Tripathi, Swarnendu, Portman, John J
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	United States 17.02.2009
Predmet:	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
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