Next Article in Journal
The Optimal Radiation Dose to Induce Robust Systemic Anti-Tumor Immunity
Next Article in Special Issue
Molecular Dynamics Simulations of Wild Type and Mutants of SAPAP in Complexed with Shank3
Previous Article in Journal
The Potential Role of a Soluble γ-Chain Cytokine Receptor as a Regulator of IL-7-Induced Lymphoproliferative Disorders
Previous Article in Special Issue
Theoretical Study on Zearalenol Compounds Binding with Wild Type Zearalenone Hydrolase and V153H Mutant
Article Menu
Issue 11 (November) cover image

Export Article

Open AccessArticle
Int. J. Mol. Sci. 2018, 19(11), 3376;

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

Institute of Mechanics, Moscow University, 1 Mitchurinsky prosp., 119234 Moscow, Russia
Institute of Immunology and Physiology, Ural Branch of Russian Academy of Sciences, 106 Pervomayskaya ul., 620049 Yekaterinburg, Russia
Author to whom correspondence should be addressed.
Received: 26 September 2018 / Revised: 24 October 2018 / Accepted: 25 October 2018 / Published: 28 October 2018
(This article belongs to the Special Issue Molecular Dynamics Simulations)
PDF [2014 KB, uploaded 1 November 2018]


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 with previous experimental observations. However, at 40 °C, the cross-linking caused a decrease in Tpm stiffness and a significant reduction in the number of main chain hydrogen bonds in the vicinity of residues 133 and 134. These data are in line with observations showing enhanced thermal unfolding of the least stable part of Tpm at 30–40 °C and accelerated trypsin cleavage at residue 133 at 40 °C (but not at 27 °C) upon cross-linking. These results allow us to speculate about the possible mechanism of involvement of Tpm cross-linking to heart failure pathogenesis. View Full-Text
Keywords: tropomyosin; disulfide bond; molecular dynamics; bending stiffness; hydrogen bonds tropomyosin; disulfide bond; molecular dynamics; bending stiffness; hydrogen bonds

Graphical abstract

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

Koubassova, N.A.; Bershitsky, S.Y.; Tsaturyan, A.K. Effects of an Interchain Disulfide Bond on Tropomyosin Structure: A Molecular Dynamics Study. Int. J. Mol. Sci. 2018, 19, 3376.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top