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• W2018441711 abstract "Myomesin is one of the most important structural molecules constructing the M-band in the force-generating unit of striated muscle, and a critical structural maintainer of the sarcomere. Using molecular dynamics simulations, we here dissect the mechanical properties of the structurally known building blocks of myomesin, namely α-helices, immunoglobulin (Ig) domains, and the dimer interface at myomesin's 13th Ig domain, covering the mechanically important C-terminal part of the molecule. We find the interdomain α-helices to be stabilized by the hydrophobic interface formed between the N-terminal half of these helices and adjacent Ig domains, and, interestingly, to show a rapid unfolding and refolding equilibrium especially under low axial forces up to ∼ 15 pN. These results support and yield atomic details for the notion of recent atomic-force microscopy experiments, namely, that the unique helices inserted between Ig domains in myomesin function as elastomers and force buffers. Our results also explain how the C-terminal dimer of two myomesin molecules is mechanically outperforming the helices and Ig domains in myomesin and elsewhere, explaining former experimental findings. This study provides a fresh view onto how myomesin integrates elastic helices, rigid immunoglobulin domains, and an extraordinarily resistant dimer into a molecular structure, to feature a mechanical hierarchy that represents a firm and yet extensible molecular anchor to guard the stability of the sarcomere." @default.
• W2018441711 created "2016-06-24" @default.
• W2018441711 creator A5047278123 @default.
• W2018441711 creator A5054677759 @default.
• W2018441711 date "2014-08-01" @default.
• W2018441711 modified "2023-10-04" @default.
• W2018441711 title "Molecular Basis of the Mechanical Hierarchy in Myomesin Dimers for Sarcomere Integrity" @default.
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• W2018441711 doi "https://doi.org/10.1016/j.bpj.2014.06.043" @default.
• W2018441711 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4142248" @default.
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