Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/97373
Title: Why muscle is an efficient shock absorber
Authors: Bershitsky, Sergey Y.
Koubassova, Natalia A.
Kopylova, Galina V.
Fernandez, Manuel
Narayanan, Theyencheri
Tsaturyan, Andrey K.
Ferenczi, Michael Alan
Keywords: DRNTU::Engineering::Mechanical engineering
Issue Date: 2014
Source: Ferenczi, M. A., Bershitsky, S. Y., Koubassova, N. A., Kopylova, G. V., Fernandez, M., Narayanan, T., et al. (2014). Why Muscle is an Efficient Shock Absorber. PLoS ONE, 9(1), e85739-.
Series/Report no.: PLoS ONE
Abstract: Skeletal muscles power body movement by converting free energy of ATP hydrolysis into mechanical work. During the landing phase of running or jumping some activated skeletal muscles are subjected to stretch. Upon stretch they absorb body energy quickly and effectively thus protecting joints and bones from impact damage. This is achieved because during lengthening, skeletal muscle bears higher force and has higher instantaneous stiffness than during isometric contraction, and yet consumes very little ATP. We wish to understand how the actomyosin molecules change their structure and interaction to implement these physiologically useful mechanical and thermodynamical properties. We monitored changes in the low angle x-ray diffraction pattern of rabbit skeletal muscle fibers during ramp stretch compared to those during isometric contraction at physiological temperature using synchrotron radiation. The intensities of the off-meridional layer lines and fine interference structure of the meridional M3 myosin x-ray reflection were resolved. Mechanical and structural data show that upon stretch the fraction of actin-bound myosin heads is higher than during isometric contraction. On the other hand, the intensities of the actin layer lines are lower than during isometric contraction. Taken together, these results suggest that during stretch, a significant fraction of actin-bound heads is bound non-stereo-specifically, i.e. they are disordered azimuthally although stiff axially. As the strong or stereo-specific myosin binding to actin is necessary for actin activation of the myosin ATPase, this finding explains the low metabolic cost of energy absorption by muscle during the landing phase of locomotion.
URI: https://hdl.handle.net/10356/97373
http://hdl.handle.net/10220/19605
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0085739
Schools: Lee Kong Chian School of Medicine (LKCMedicine) 
Rights: © 2014 Ferenczi et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:LKCMedicine Journal Articles

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