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

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

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 prop...

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Bibliographic Details
Main Authors: Natalia A. Koubassova, Sergey Y. Bershitsky, Andrey K. Tsaturyan
Format: Article
Language:English
Published: MDPI AG 2018-10-01
Series:International Journal of Molecular Sciences
Subjects:
tropomyosin
disulfide bond
molecular dynamics
bending stiffness
hydrogen bonds
Online Access:https://www.mdpi.com/1422-0067/19/11/3376

Internet

https://www.mdpi.com/1422-0067/19/11/3376

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