Abstract
The description of the molecular events that produce tension in a contracting muscle is often called mechanochemistry, a term that well describes the synthesis of the two key elements in the contractile cycle. One of those elements is mechanical: we need to be able to describe in detail, with resolution down to the atomic level, the sequence of conformational changes that cause the thick and thin filaments to slide past one another. The other element is chemical: we need to determine the sequence of biochemical reactions in the contractile cycle and to measure the energetic and kinetic parameters of each of those reactions. Finally, the problem requires synthesis: we need to explain the coupling of the mechanical and chemical events. Only then will we understand how the chemical energy released by the hydrolysis of ATP is converted to the mechanical work performed by the contracting muscle.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Belford, G. G., Beiford, R. L., and Weber, G., 1972, Dynamics of fluorescence polarization in macromolecules, Proc. Natl. Acad. Sci. U.S.A. 69:1392.
Borejdo, J., Putnam, S., and Morales, M. F., 1979, Fluctuations in polarized fluorescence: Evidence that muscle cross bridges rotate repetitively during contraction, Proc. Natl. Acad. Sci. U.S.A. 76:6346.
Bressler, B. H., and Clinch, N. F., 1975, Cross bridges as the major source of compliance in contracting skeletal muscle, Nature (London) 256:221.
Broersma, S., 1960, Rotational diffusion of a cylindrical particle, J. Chem. Phys. 32:1626.
Bull, H. B., and Breese, K., 1973, Thermal transitions of proteins, Arch. Biochem. Biophys. 156:604.
Burke, M., Himmelfarb, S., and Harrington, W. F., 1973, Studies on the “hinge” region of myosin, Biochemistry 12:701.
Chiao, Y.-C. C., and Harrington, W. F., 1979, Cross-bridge movement in glycerinated rabbit psoas muscle fibers, Biochemistry 18:959.
Dalton, L. R., 1976, Saturation transfer spectroscopy, Adv. Magn. Reson. 8:149.
Eisenberg, E., and Hill, T. L., 1978, A cross-bridge model of muscle contraction, Prog. Biophys. Mol. Biol. 33:55.
Eisenberg, E., Hill, T. L., and Chen, Y. D., 1980, Cross-bridge model of muscle contraction: Quantitative analysis, Biophys. J. 29:195.
Elliott, A., and Offer, G., 1978, Shape and flexibility of the myosin molecule, J. Mol. Biol. 123:505.
Flory, P. J., 1956, Role of crystallization in polymers and proteins, Science 124:53.
García Bernai, J. M., and García de la Torre, J., 1980, Transport properties and hydrodynamic centers of rigid macromolecules with arbitrary shapes, Biopolymers 19:751.
García de la Torre, J., and Bloomfield, V. A., 1978, Hydrodynamic properties of macromolecular complexes. IV. Intrinsic viscosity theory, with applications to once-broken rods and mul-tisubunit proteins, Biopolymers 17:1605.
García de la Torre, J., and Bloomfield, V. A., 1980, Conformation of myosin in dilute solution as estimated from hydrodynamic properties, Biochemistry 19:5118.
Goodno, C. C., and Swenson, C. A., 1975a, Thermal transitions of myosin and its helical fragments. I. Shifts in proton equilibria accompanying unfolding, Biochemistry 14:867.
Goodno, C. C., and Swenson, C. A., 1975b, Thermal transitions of myosin and its helical fragments. II. Solvent-induced variations in conformational stability, Biochemistry 14:873.
Goodno, C. C., Harris, T. A., and Swenson, C. A., 1976, Thermal transitions of myosin and its helical fragments: Regions of structural instability in the myosin molecule, Biochemistry 15:5157.
Harrington, W. F., 1971, A mechanochemical mechanism for muscle contraction, Proc. Natl. Acad. Sci. U.S.A. 68:685.
Harvey, S. C., and Cheung, H. C., 1972, Computer simulation of fluorescence depolarization due to Brownian motion, Proc. Natl. Acad. Sci. U.S.A. 69:3670.
Harvey, S. C., and Cheung, H. C., 1977, Fluorescence depolarization studies on the flexibility of the myosin rod, Biochemistry 16:5181.
Harvey, S. C., and Cheung, H. C., 1980, Transport properties of particles with segmental flexibility. II. Decay of fluorescence polarization anisotropy from hinged macromolecules, Biopolymers 19:913.
Harvey, S. C., Cheung, H. C., and Thames, K. E., 1977, Cooperativity in F-actin filaments on binding of myosin subfragments, demonstrated by fluorescence of l,N 6-ethenoadenosine diphosphate, Arch. Biochem. Biophys. 179:391.
Haselgrove, J. C., and Huxley, H. E., 1973, X-ray evidence for radial crossbridge movement and for the sliding filament model in actively contracting skeletal muscle, J. Mol. Biol. 77:549.
Haselgrove, J. C., Stewart, M., and Huxley, H. E., 1976, Cross-bridge movement during muscle contraction, Nature (London) 261:606.
Highsmith, S., 1978, The effects of divalent cations on the rotational mobility of myosin, heavy meromyosin and myosin subfragment-1 and on the binding of heavy meromyosin to actin, Biochim. Biophys. Acta 536:156.
Highsmith, S., Kretzschmar, K. M., O’Konski, C. T., and Morales, M. F., 1977, Flexibility of myosin rod, light meromyosin, and myosin subfragment-2 in solution, Proc. Natl. Acad. Sci. U.S.A. 74:4986.
Highsmith, S., Akasaka, K., Konrad, M., Goody, R., Holmes, K., Wade-Jardetzky, N., and Jardetzky, O., 1979, Internal motions in myosin, Biochemistry 18:4238.
Huxley, A. F., and Simmons, R. M., 1971, Proposed mechanism of force generation in striated muscle, Nature (London) 233:533.
Huxley, H. E., 1957, The double array of filaments in cross-striated muscle, J. Biophys. Biochem. Cytol. 3:631.
Huxley, H. E., 1969, The mechanism of muscle contraction, Science 164:1356.
Huxley, H. E., 1971, The structural basis of muscular contraction, Proc. R. Soc. London Ser. B 160:442.
Huxley, H. E., and Brown, W., 1967, The low-angle X-ray diagram of vertebrate striated muscle and its behavior during contraction and rigor, J. Mol. Biol. 30:383.
Hyde, J. S., 1978, Saturation transfer spectroscopy, Methods Enzymol. 49:480.
King, M. V., 1976, Electron-microscopic mapping of the hinge region of myosin, Experientia 32:975.
Kobayashi, S., and Totsuka, T., 1975, Electric birefringence of myosin subfragments, Biochim. Biophys. Acta 376:375.
Lowey, S., Slayter, H. S., Weeds, A. G., and Baker, H., 1969, Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation, J. Mol. Biol. 42:1.
Lymn, R. W., 1975, Equatorial X-ray reflections and cross arm movement in skeletal muscle, Nature (London) 258:770.
Mannherz, H. G., and Goody, R. S., 1976, Proteins of contractile systems, Annu. Rev. Biochem. 45:427.
Margossian, S. S., and Lowey, S., 1973, Substructure of the myosin molecule. IV. Interactions of myosin and its subfragments with adenosine triphosphate and F-actin, J. Mol. Biol. 74:313.
Marston, S. B., Treagear, R. T., Rodger, C. D., and Clarke, M. L., 1979, Coupling between the enzymatic site of myosin and the mechanical output of muscle, J. Mol. Biol. 128:111.
Mendelson, R. A., and Cheung, P., 1976, Muscle crossbridges: Absence of direct effect of calcium on movement away from the thick filaments, Science 194:190.
Mendelson, R. A., and Cheung, P. H.-C, 1978, Intrinsic segmental flexibility of the S-l moiety of myosin using single-headed myosin, Biochemistry 17:2139.
Mendelson, R. A., Mowery, P. C., Botts, J., and Cheung, H. C., 1972, The segmental flexibility of the S-l moiety of myosin, Biophys. J. 12:281a.
Mendelson, R. A., Morales, M. F., and Botts, J., 1973, Segmental flexibility of the S-l moiety of myosin, Biochemistry 12:2250.
Morales, M. F., and Botts, J., 1979, On the molecular basis for chemomechanical energy transduction in muscle, Proc. Natl. Acad. Sci. U.S.A.76:3857.
Murphy, R. A., 1979, Filament organization and contractile function in vertebrate smooth muscle, Annu. Rev. Physiol. 41:737.
Nakajima, H., and Wada, Y., 1977, A general method for evaluation of diffusion constants, dilute-solution viscoelasticity, and the dielectric property of a rigid macromolecule with an arbitrary conformation. I, Biopolymers 16:875.
Peller, L., 1975, Segmental flexibility in the myosin molecule: Evidence from binding studies of myosin fragments with actin, J. Supramol. Struct. 3:169.
Perrin, F., 1934, Mouvement Brownien d’un ellipsoide. I. Dispersion diélectrique pour des molécules ellipsoidales,J. Phys. Radium VII 5:497.
Perrin, F., 1936, Mouvement Brownien d’un ellipsoide. IL Rotation libre et dépolarisation des fluorescences: Translation et diffusion de molécules ellipsoidales, J. Phys. Radium VII 7:1.
Rosser, R. W., Schrag, J. L., Ferry, J. D., and Greaser, M., 1977, Viscoelastic properties of very dilute paramyosin solutions, Macromolecules 10:978.
Rosser, R. W., Nestler, F. H. M., Schrag, J. L., Ferry, J. D., and Greaser, M., 1978, Infinite-dilution viscoelastic properties of myosin, Macromolecules 11:1239.
Samejima, K., Takahashi, K., and Yasui, T., 1976, Heat-induced denaturation of myosin total rod, Agric. Biol. Chem. 40:2455.
Schoenberg, M., 1980a, Geometrical factors influencing muscle force development. I. The effect of filament spacing upon axial forces, Biophys. J. 30:51.
Schoenberg, M., 1980b, Geometrical factors influencing muscle force development. II. Radial forces, Biophys. J. 30:69.
Squire, J. M., 1975, Muscle filament structure and muscle contraction, Annu. Rev. Biophys. Bioeng. 4:137.
Sutoh, K., and Harrington, W. F., 1977, Cross-linking of myosin thick filaments under activating and rigor conditions: A study of the radial disposition of the cross-bridges, Biochemistry 16:2441.
Sutoh, K., Sutoh, K., Karr, T., and Harrington, W. F., 1978a, Isolation and physico-chemical properties of a high molecular weight subfragment-2 of myosin, J. Mol. Biol. 126:1.
Sutoh, K., Chiao, Y.-C. C., and Harrington, W. F., 1978b, Effect of pH on the cross-bridge arrangement in synthetic myosin filaments, Biochemistry 17:1234.
Takahashi, K., 1978, Topography of the myosin molecule as visualized by an improved negative staining method, J. Biochem. 83:905.
Taylor, E., 1979, Mechanism of actomyosin ATPase and the problem of muscle contraction, CRC Crit. Revs. Biochem. 6:103.
Thomas, D. D., 1978, Large scale rotational motions of proteins detected by electron paramagnetic resonance and fluorescence, Biophys. J. 24:439.
Thomas, D. D., Seidel, J. C., Gergely, J., and Hyde, J. S., 1975a, The quantitative measurement of rotational motion of the subfragment-1 region of myosin by saturation transfer EPR spectroscopy, J. Supramol. Struct. 3:376.
Thomas, D. D., Seidel, J. C., Hyde, J. S., and Gergely, J., 1975b, Motion of subfragment-1 in myosin and its supramolecular complexes: Saturation transfer electron paramagnetic resonance, Proc. Natl. Acad. Sci. U.S.A. 72:1729.
Thomas, D. D., Dalton, L. R., and Hyde, J. S., 1976, Rotational diffusion studied by passage saturation transfer electron paramagnetic resonance, J. Chem. Phys. 65:3006.
Tsong, T. Y., Karr, T., and Harrington, W. F., 1979, Rapid helix-coil transitions in the S-2 region of myosin, Proc. Natl. Acad. Sci. U.S.A. 76:1109.
Wahl, P., 1975, Decay of fluorescence anisotropy, in: Biochemical Fluorescence: Concepts (R. F. Chen and H. Edelhoch, eds.), pp. 1–41, Marcel Dekker, New York.
Weber, A., and Murray, J. M., 1973, Molecular control mechanisms in muscle contraction, Physiol. Rev. 53:612.
Yguerabide, J., 1972, Nanosecond fluorescence spectroscopy of macromolecules, Methods En-zymol. 26C:498.
Yguerabide, J., Epstein, H. F., and Stryer, L., 1970, Segmental flexibility in an antibody molecule, J. Mol. Biol. 51:573.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1982 Plenum Press, New York
About this chapter
Cite this chapter
Harvey, S.C., Cheung, H.C. (1982). Myosin Flexibility. In: Dowben, R.M., Shay, J.W. (eds) Cell and Muscle Motility. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-4037-9_20
Download citation
DOI: https://doi.org/10.1007/978-1-4684-4037-9_20
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-4039-3
Online ISBN: 978-1-4684-4037-9
eBook Packages: Springer Book Archive