Including Thermal Fluctuations in Actomyosin Stable States Increases the Predicted Force per Motor and Macroscopic Efficiency in Muscle Modelling.

Bibliographic Details
Title: Including Thermal Fluctuations in Actomyosin Stable States Increases the Predicted Force per Motor and Macroscopic Efficiency in Muscle Modelling.
Authors: Lorenzo Marcucci, Takumi Washio, Toshio Yanagida
Source: PLoS Computational Biology, Vol 12, Iss 9, p e1005083 (2016)
Publisher Information: Public Library of Science (PLoS), 2016.
Publication Year: 2016
Collection: LCC:Biology (General)
Subject Terms: Biology (General), QH301-705.5
More Details: Muscle contractions are generated by cyclical interactions of myosin heads with actin filaments to form the actomyosin complex. To simulate actomyosin complex stable states, mathematical models usually define an energy landscape with a corresponding number of wells. The jumps between these wells are defined through rate constants. Almost all previous models assign these wells an infinite sharpness by imposing a relatively simple expression for the detailed balance, i.e., the ratio of the rate constants depends exponentially on the sole myosin elastic energy. Physically, this assumption corresponds to neglecting thermal fluctuations in the actomyosin complex stable states. By comparing three mathematical models, we examine the extent to which this hypothesis affects muscle model predictions at the single cross-bridge, single fiber, and organ levels in a ceteris paribus analysis. We show that including fluctuations in stable states allows the lever arm of the myosin to easily and dynamically explore all possible minima in the energy landscape, generating several backward and forward jumps between states during the lifetime of the actomyosin complex, whereas the infinitely sharp minima case is characterized by fewer jumps between states. Moreover, the analysis predicts that thermal fluctuations enable a more efficient contraction mechanism, in which a higher force is sustained by fewer attached cross-bridges.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 1553-734X
1553-7358
Relation: http://europepmc.org/articles/PMC5023195?pdf=render; https://doaj.org/toc/1553-734X; https://doaj.org/toc/1553-7358
DOI: 10.1371/journal.pcbi.1005083
Access URL: https://doaj.org/article/ef9d7de5e6434d27abc50761e07b482b
Accession Number: edsdoj.f9d7de5e6434d27abc50761e07b482b
Database: Directory of Open Access Journals
More Details
ISSN:1553734X
15537358
DOI:10.1371/journal.pcbi.1005083
Published in:PLoS Computational Biology
Language:English