Effects of an Interchain Disulfide Bond on Tropomyosin Structure: A Molecular Dynamics Study.

ABSTRACT: Tropomyosin (Tpm) is a coiled-coil actin-binding dimer protein that participates in the regulation of muscle contraction. Both Tpm chains contain Cys190 residues which are normally in the reduced state, but form an interchain disulfide bond in failing heart. Changes in structural and functional properties of Tpm and its complexes with actin upon disulfide cross-linking were studied using various experimental methods. To understand the molecular mechanism underlying these changes and to reveal the possible mechanism of the involvement of the cross-linking in heart failure, molecular dynamics (MD) simulations of the middle part of Tpm were performed in cross-linked and reduced states. The cross-linking increased bending stiffness of Tpm assessed from MD trajectories at 27 °C in agreement wit

SUBMITTER: Koubassova NA 

PROVIDER: S-EPMC6274839 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature