Actomyosin interaction: mechanical and energetic properties in different nucleotide binding states.

ABSTRACT: The mechanics of the actomyosin interaction is central in muscle contraction and intracellular trafficking. A better understanding of the events occurring in the actomyosin complex requires the examination of all nucleotide-dependent states and of the energetic features associated with the dynamics of the cross-bridge cycle. The aim of the present study is to estimate the interaction strength between myosin in nucleotide-free, ATP, ADP.Pi and ADP states and actin monomer. The molecular models of the complexes were constructed based on cryo-electron microscopy maps and the interaction properties were estimated by means of a molecular dynamics approach, which simulate the unbinding of the complex applying a virtual spring to the core of myosin protein. Our results suggest that during an ATP

SUBMITTER: Aprodu I 

PROVIDER: S-EPMC2635604 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature