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Current Chinese Science

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ISSN (Print): 2210-2981
ISSN (Online): 2210-2914

Research Article Section: Biochemistry

The Mechanism of Energy Changes That Occur Depending on the Ratio of Force and Speed in The Example of Bicycle Ergometric Testing

Author(s): Nedotsuk Yura and Aleksej Laptev*

Volume 4, Issue 2, 2024

Published on: 30 November, 2023

Page: [95 - 105] Pages: 11

DOI: 10.2174/0122102981260447231115115150

Price: $65

Open Access Journals Promotions 2
Abstract

Introduction: For the first time, in the aspect of biophysics, the reasons for the increase in the power of the threshold of anaerobic metabolism developed by the test person during functional diagnostics.

Methods: This occurs with an increase in the pedaling frequency with which the specified load on a bicycle ergometer in the range from 40 to 140 rpm (0.73-2.56 m/s) is overcome, have been substantiated.

Results: It was determined that the ratio of force and velocity in the studied range of pedaling frequencies (muscle contractile speed) corresponds to the hyperbolic type with displaced axes.

Conclusion: At the same time, with an increase in pedaling frequency, power increases in a cubic dependence, and the rate of oxygen consumption by the test subject decreases linearly in the process of overcoming the same fixed-power load set on a bicycle ergometer and vice versa.

Keywords: Energy fluctuations, force-speed dependence, aerobic performance, the threshold of anaerobic metabolism, actomyosin complex, functional diagnostics.

Graphical Abstract
[1]
Nedotsuk, Yu.I.; Laptev, A.I.; Lobanov, E.V.; Levushkin, S.P. Substantiation of the need to take into account latent energy costs arising in the process of bicycle ergometry in order to correctly determine the energy potential of the tested. In: Scientific notes of the University. P.F. Lesgaft. No; , 2019; 3, pp. 226-234.
[2]
Nedotsuk, Yu.I.; Laptev, A.I. The effect of pedaling frequency on the power of the anaerobic threshold. Part 1. Bulletin of Sports Science, 2021, (5), 18-24.
[3]
Nedotsuk, Yu.I.; Laptev, A.I. The effect of pedaling frequency on the power of the anaerobic threshold. Part 2. Bulletin of Sports Science, 2021, (6), 38-41.
[4]
Nedotsuk, Yu.I.; Laptev, A.I. Universal ergometric complex as a tool for the correct determination of developed power when using bicycle ergometers in the process of functional testing. J. Sport Health Sci., 2022, 5, 40-48.
[5]
Hill, A.V. The heat of shortening and the dynamic constants of muscle. Proc. R. Soc. Lond. B Biol. Sci., 1938, 126(843), 136-195.
[http://dx.doi.org/10.1098/rspb.1938.0050]
[6]
Hill, T.L.; White, G.M. On the sliding-filament model of muscular contraction, IV. Calculation of force-velocity curves. Proc. Natl. Acad. Sci., 1968, 61(3), 889-896.
[http://dx.doi.org/10.1073/pnas.61.3.889] [PMID: 5246550]
[7]
Månsson, A.; Ušaj, M.; Moretto, L.; Rassier, D. Do actomyosin single-molecule mechanics data predict mechanics of contracting muscle? Int. J. Mol. Sci., 2018, 19(7), 1863.
[http://dx.doi.org/10.3390/ijms19071863] [PMID: 29941816]
[8]
Kaya, M.; Higuchi, H. Nonlinear elasticity and an 8-nm working stroke of single myosin molecules in myofilaments. Science, 2010, 329(5992), 686-689.
[http://dx.doi.org/10.1126/science.1191484] [PMID: 20689017]
[9]
Nocella, M.; Bagni, M.A.; Cecchi, G.; Colombini, B. Mechanism of force enhancement during stretching of skeletal muscle fibres investigated by high time-resolved stiffness measurements. J. Muscle Res. Cell Motil., 2013, 34(1), 71-81.
[http://dx.doi.org/10.1007/s10974-012-9335-4] [PMID: 23296372]
[10]
Lewalle, A.; Steffen, W.; Stevenson, O.; Ouyang, Z.; Sleep, J. Single-molecule measurement of the stiffness of the rigor myosin head. Biophys. J., 2008, 94(6), 2160-2169.
[http://dx.doi.org/10.1529/biophysj.107.119396] [PMID: 18065470]
[11]
Piazzesi, G.; Reconditi, M.; Linari, M.; Lucii, L.; Bianco, P.; Brunello, E.; Decostre, V.; Stewart, A.; Gore, D.B.; Irving, T.C.; Irving, M.; Lombardi, V. Skeletal muscle performance determined by modulation of number of myosin motors rather than motor force or stroke size. Cell, 2007, 131(4), 784-795.
[http://dx.doi.org/10.1016/j.cell.2007.09.045] [PMID: 18022371]
[12]
Aksel, T.; Choe Yu, E.; Sutton, S.; Ruppel, K.M.; Spudich, J.A. Ensemble force changes that result from human cardiac myosin mutations and a small-molecule effector. Cell Rep., 2015, 11(6), 910-920.
[http://dx.doi.org/10.1016/j.celrep.2015.04.006] [PMID: 25937279]
[13]
Månsson, A. Actomyosin based contraction: One mechanokinetic model from single molecules to muscle? J. Muscle Res. Cell Motil., 2016, 37(6), 181-194.
[http://dx.doi.org/10.1007/s10974-016-9458-0] [PMID: 27864648]
[14]
Sung, J.; Nag, S.; Mortensen, K.I.; Vestergaard, C.L.; Sutton, S.; Ruppel, K.; Flyvbjerg, H.; Spudich, J.A. Harmonic force spectroscopy measures load-dependent kinetics of individual human β-cardiac myosin molecules. Nat. Commun., 2015, 6(1), 7931.
[http://dx.doi.org/10.1038/ncomms8931] [PMID: 26239258]
[15]
Mentes, A.; Huehn, A.; Liu, X.; Zwolak, A.; Dominguez, R.; Shuman, H.; Ostap, E.M.; Sindelar, C.V. High-resolution cryo-EM structures of actin-bound myosin states reveal the mechanism of myosin force sensing. Proc. Natl. Acad. Sci., 2018, 115(6), 1292-1297.
[http://dx.doi.org/10.1073/pnas.1718316115] [PMID: 29358376]
[16]
Barclay, C.J. Estimation of cross-bridge stiffness from maximum thermodynamic efficiency. J. Muscle Res. Cell Motil., 1998, 19(8), 855-864.
[http://dx.doi.org/10.1023/A:1005409708838] [PMID: 10047985]
[17]
Bradshaw, M.; Paul, D.M. After the revolution: How is Cryo-EM contributing to muscle research? J. Muscle Res. Cell Motil., 2019, 40(2), 93-98.
[http://dx.doi.org/10.1007/s10974-019-09537-7] [PMID: 31302812]
[18]
Sung, J.; Mortensen, K.I.; Spudich, J.A.; Flyvbjerg, H. How to measure load-dependent kinetics of individual motor molecules without a force-clamp. Methods Enzymol., 2017, 582, 1-29.
[http://dx.doi.org/10.1016/bs.mie.2016.08.002] [PMID: 28062031]
[19]
Piazzesi, G.; Lucii, L.; Lombardi, V. The size and the speed of the working stroke of muscle myosin and its dependence on the force. J. Physiol., 2002, 545(1), 145-151.
[http://dx.doi.org/10.1113/jphysiol.2002.028969] [PMID: 12433956]
[20]
Houdusse, A.; Sweeney, H.L. How myosin generates force on actin filaments. Trends Biochem. Sci., 2016, 41(12), 989-997.
[http://dx.doi.org/10.1016/j.tibs.2016.09.006] [PMID: 27717739]
[21]
Alcazar, J.; Csapo, R.; Ara, I.; Alegre, L.M. On the shape of the force-velocity relationship in skeletal muscles: The linear, the hyperbolic, and the double-hyperbolic. Front. Physiol., 2019, 10, 769.
[http://dx.doi.org/10.3389/fphys.2019.00769] [PMID: 31275173]
[22]
Romanovsky, Yu.M.; Tikhonov, A.N. Molecular converters of energy of living cell. Proton ATF-sintaza - the rotating molecular motor. UFN, 2010, 180(9), 931-956.
[http://dx.doi.org/10.3367/UFNr.0180.201009b.0931]

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