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...

Ausführliche Beschreibung

Bibliographische Detailangaben

Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS Jg. 106; H. 7; S. 2104
Hauptverfasser:	Tripathi, Swarnendu, Portman, John J
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	United States 17.02.2009
Schlagworte:	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-Zugang:	Weitere Angaben
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!