Dynamics of the coiled-coil unfolding transition of myosin rod probed by dissipation force spectrum.

Biophysical Journal
Yukinori TaniguchiMasaru Kawakami

Abstract

The motor protein myosin II plays a crucial role in muscle contraction. The mechanical properties of its coiled-coil region, the myosin rod, are important for effective force transduction during muscle function. Previous studies have investigated the static elastic response of the myosin rod. However, analogous to the study of macroscopic complex fluids, how myosin will respond to physiological time-dependent loads can only be understood from its viscoelastic response. Here, we apply atomic force microscopy using a magnetically driven oscillating cantilever to measure the dissipative properties of single myosin rods that provide unique dynamical information about the coiled-coil structure as a function of force. We find that the friction constant of the single myosin rod has a highly nontrivial variation with force; in particular, the single-molecule friction constant is reduced dramatically and increases again as it passes through the coiled-uncoiled transition. This is a direct indication of a large free-energy barrier to uncoiling, which may be related to a fine-tuned dynamic mechanosignaling response to large and unexpected physiological loads. Further, from the critical force at which the minimum in friction occurs we dete...Continue Reading

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Citations

Aug 27, 2013·Journal of Biological Physics·Katarzyna E Małek, Robert Szoszkiewicz
Sep 28, 2014·Biochimica Et Biophysica Acta·Matthew BatchelorEmanuele Paci
Jul 10, 2012·Biophysical Journal·Akiko Ikeda-KobayashiMasaru Kawakami
Jul 25, 2012·Biophysical Journal·Christian M KaiserAndres F Oberhauser
Feb 17, 2012·Biophysics·Yukinori TaniguchiMasaru Kawakami
Dec 12, 2012·Chemical Society Reviews·Ali Miserez, Paul A Guerette
Jun 15, 2018·Chemical Science·Melis GoktasKerstin G Blank
May 5, 2018·Langmuir : the ACS Journal of Surfaces and Colloids·Hila NadlerRonen Berkovich

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