Coiled-coil nanomechanics and uncoiling and unfolding of the superhelix and α-helices of myosin

Douglas D. Root, Vamsi K. Yadavalli, Jeffrey G. Forbes, Kuan Wang

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

The nanomechanical properties of the coiled-coils of myosin are fundamentally important in understanding muscle assembly and contraction. Force spectra of single molecules of double-headed myosin, single-headed myosin, and coiled-coil tail fragments were acquired with an atomic force microscope and displayed characteristic triphasic force-distance responses to stretch: a rise phase (R) and a plateau phase (P) and an exponential phase (E). The R and P phases arise mainly from the stretching of the coiled-coils, with the hinge region being the main contributor to the rise phase at low force. Only the E phase was analyzable by the worm-like chain model of polymer elasticity. Restrained molecular mechanics simulations on an existing x-ray structure of scallop S2 yielded force spectra with either two or three phases, depending on the mode of stretch. It revealed that coiled-coil chains separate completely near the end of the P phase and the stretching of the unfolded chains gives rise to the E phase. Extensive conformational searching yielded a P phase force near 40 pN that agreed well with the experimental value. We suggest that the flexible and elastic S2 region, particularly the hinge region, may undergo force-induced unfolding and extend reversibly during actomyosin powerstroke.

Original languageEnglish
Pages (from-to)2852-2866
Number of pages15
JournalBiophysical Journal
Volume90
Issue number8
DOIs
Publication statusPublished - Apr 2006
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics

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