Skip to main content
SpringerLink
Log in
Book cover

The Sliding-Filament Theory of Muscle Contraction pp 237–291Cite as

Myosin Motors

  • Chapter
  • First Online:

  • 1087 Accesses

Abstract

The last decade of the twentieth century was a fertile period for muscle research. Not only did it yield the atomic structures of actin and myosin-S1, but it spawned a number of new techniques, including optical trapping, evanescent wave and atomic force spectroscopies, for observing the working strokes of a single molecular motor such as myosin, kinesin and dynein. Muscle myosin II is part of a larger family of myosin motors that perform different cellular tasks. Many of them, including myosin-V, are processive motors which walk many steps along F-actin before falling off. Actin-myosin kinetics in the optical trap determine how the apparent working stroke may be affected by target zones on F-actin. Moving traps may be used to measure myosin stiffness and the lifetimes of actomyosin states as a function of load. Three critical experiments require interpretation: why does the ATP sliding distance in motility assays exceed the working stroke, why are Cy3-ATP detachment events not always coordinated with ATP binding, and why does a single myosin-II on a fine cantilever walk for several 5.3 nm steps on F-actin, which suggests that myosin moves by a ratchet mechanism rather than a swinging lever-arm. Finally, recent experiments on myosin-V suggest that its lever-arm is uniquely suited for making 36 nm steps on actin.

I came here confused about actin and myosin. Now I am still confused, but at a higher level.

Sir Andrew Huxley F.R.S., on summing up the symposium on Frontiers in Molecular Motors, Osaka, Japan, hosted by Toshio Yanagida (Cyranoski 2000).

This is a preview of subscription content, log in via an institution.

Chapter
USD   29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   129.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Hardcover Book
USD   169.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

References

  • Adamovic I, Mijailovich SM, Karplus M (2008) The elastic properties of the structurally characterized myosin II S2 subdomain: a molecular dynamics and normal mode analysis. Biophys J 94:3779–3789

    CAS  PubMed  PubMed Central  Google Scholar 

  • Ali MY, Uemura S, Adachi K, Itoh H, Kinosita K, Ishiwata S (2002) Myosin V is a left-handed spiral motor on the right-handed actin helix. Nat Struct Biol 9:464–467

    Article  CAS  PubMed  Google Scholar 

  • Astumian RD (1997) Thermodynamics and kinetics of a Brownian motor. Science 276:917–922

    Article  CAS  PubMed  Google Scholar 

  • Baker JE, Brust-Mascher I, Ramachandran S, LaConte IFW, Thomas DD (1998) A large and distinct rotation of the myosin light chain domain occurs upon muscle contraction. Proc Natl Acad Sci USA 95:2944–2949

    CAS  PubMed  PubMed Central  Google Scholar 

  • Bell GI (1978) Models for the specfic adhesion of cells to cells. Science 200:618–627

    Article  CAS  PubMed  Google Scholar 

  • Berg JS, Powell BC, Cheney RE (2001) A millennial myosin census. Mol Biol Cell 12:780–794

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Block SM, Svoboda K (1995) Analysis of high-resolution recordings of motor movement. Biophys J 68:230S–241S

    CAS  PubMed  PubMed Central  Google Scholar 

  • Bourdieu L, Duke T, Elowitz MB, Winkelmann DA, Leibler S, Libchaber A (1995) Spiral defects in motility assays: a measure of motor protein force. Phys Rev Lett 75:176–179

    Article  CAS  PubMed  Google Scholar 

  • Bozic SM (1979) Digital and Kalman Filtering. Edward Arnold, London

    Google Scholar 

  • Brenner B (1991) Rapid dissociation and reassociation of actomyosin crossbridges during force generation: a newly observed facet of cross-bridge action in muscle. Proc Natl Acad Sci USA 88:10490–10494

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Brenner B (2006) The stroke size of myosins: a reevaluation. J Muscle Res Cell Motil 27:173–187

    Article  CAS  PubMed  Google Scholar 

  • Bruno WJ, Ullah G, Mak D-OD, Pearson JE (2013) Automated maximum likelihood separation of signal from baseline in noisy quantal data. Biophys J 105:68–79

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Burton K (1992) Myosin step size: estimates from motility assays and shortening muscle. J Muscle Res Cell Motil 13:590–607

    Article  CAS  PubMed  Google Scholar 

  • Capitanio M, Canepari M, Cacciafesta P, Lombardi V, Cicchi R, Maffei M, Pavone FS, Bottinelli R (2006) Two independent mechanical events in the interaction cycle of skeletal muscle myosin with actin. Proc Natl Acad Sci USA 103:87–92

    Article  CAS  PubMed  Google Scholar 

  • Capitanio M, Canepari M, Maffei M, Beneventi D, Monico C, Vanzi F, Bottinelli R, Pavone FS (2012) Ultrafast force-clamp spectroscopy of single molecules reveals load dependence of myosin working stroke. Nat Methods 9:1013–1019

    Article  CAS  PubMed  Google Scholar 

  • Carter BC, Vershinin M, Gross SP (2008) A comparison of step-detection methods: how well can you do? Biophys J 94:306–319

    Article  CAS  PubMed  Google Scholar 

  • Chandrasekhar S (1943) Stochastic problems in physics and astronomy. Rev Mod Phys 15:1–89

    Article  Google Scholar 

  • Chung SH, Kennedy RA (1991) Forward-backward non-linear filtering technique for extracting small biological signals from noise. J Neurosci Methods 40:71–86

    Article  CAS  PubMed  Google Scholar 

  • Colquhoun D (1998) In: Sakmann E, Neher E (eds) Single-channel recording. Plenum, New York/London

    Google Scholar 

  • Coureux PD, Wells AL, Menetrey J, Yengo CM, Morris CA, Sweeney HL (2004) Three myosin V structures delineate essential features of chemo-mechanical transduction. EMBO J 23:4527–4537

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Cyranoski D (2000) Swimming against the tide. Nature 408:764–766

    Article  CAS  PubMed  Google Scholar 

  • De La Cruz E, Ostap EM (2004) Relating biochemistry and function in the myosin superfamily. Curr Opin Cell Biol 16:61–67

    Article  PubMed  CAS  Google Scholar 

  • Finer JT, Simmons RM, Spudich JA (1994) Single myosin molecule mechanics: piconewton forces and nanometer steps. Nature 368:113–119

    Article  CAS  PubMed  Google Scholar 

  • Forkey JN, Quinlan ME, Shaw MA, Corrie JET, Goldman YE (2003) Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization. Nature 422:399–404

    Article  CAS  PubMed  Google Scholar 

  • Fortune NS, Ranatunga KW, Geeves MA (1994) The influence of 2,3-butanedione 2-monoxime (BDM) on the interaction between actin and myosin in solution and in skinned muscle fibres. J Muscle Res Cell Motil 15:309–318

    PubMed  Google Scholar 

  • Funatsu T, Harada Y, Tokunaga M, Saito KL, Yanagida T (1995) Imaging of single fluorescent molecules and individual ATP turnovers by singe myosin molecules in aqueous solution. Nature 374:555–559

    Article  CAS  PubMed  Google Scholar 

  • Gardiner C (2004) Handbook of stochastic methods for physics, chemistry and the natural sciences, Springer Series in Synergetics. Springer-Verlag, Berlin/New York

    Book  Google Scholar 

  • Guilford WH, Dupuis DE, Kennedy G, Wu JR, Patlak JB, Warshaw DM (1997) Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacements in the laser trap. Biophys J 72:1006–1021

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Happel J, Brenner H (1983) Low Reynolds number hydrodynamics. Martinus Nijhoff, The Hague

    Google Scholar 

  • Harada Y, Noguchi A, Kishino A, Yanagida T (1987) Sliding movement of single actin filaments on one-headed myosin filaments. Nature 326:805–808

    Article  CAS  PubMed  Google Scholar 

  • Harada Y, Sakurada K, Aoki T, Thomas DD, Yanagida T (1990) Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay. J Mol Biol 216:49–68

    Article  CAS  PubMed  Google Scholar 

  • Hartman MA, Spudich JA (2004) The myosin superfamily at a glance. J Cell Sci 125:1627–1632

    Article  CAS  Google Scholar 

  • He Z-H, Chillingworth RK, Brune M, Corrie JET, Webb MR, Ferenczi MA (1999) The efficiency of contraction in rabbit skeletal muscle fibres, determined from the rate of release of inorganic phosphate. J Physiol (London) 517(3):839–854

    Article  CAS  Google Scholar 

  • Higuchi H, Goldman YE (1991) Sliding distance between actin and myosin filaments per ATP molecule hydrolysed in skinned muscle fibres. Nature 352:352–354

    Article  CAS  PubMed  Google Scholar 

  • Hodge T, Cope JTV (2000) A myosin family tree. J Cell Sci 113:3353–3354

    CAS  PubMed  Google Scholar 

  • Howard J (2001) Mechanics of motor proteins and the cytoskeleton. Sinauer Assoc. Inc., Sunderland, p104

    Google Scholar 

  • Howard J, Spudich JA (1996) Is the lever arm of myosin a molecular elastic element? Proc Natl Acad Sci USA 93:4462–4464

    CAS  PubMed  Google Scholar 

  • Ishijima A, Kojima H, Funatsu T, Tokunaga M, Higuchi H, Tanaka H, Yanagida T (1998) Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin. Cell 92:161–171

    Article  CAS  PubMed  Google Scholar 

  • Ito K, Liu X, Katayama E, Uyeda TQP (1999) Cooperativity between two heads of Dictyostelium myosin in in vitro motility and ATP hydrolysis. Biophys J 76:985–992

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Iwaki M, Iwane AH, Shimokawa T, Cooke R, Yanagida T (2009) Brownian search and catch mechanism for myosin VI steps. Nat Chem Biol 5:403–405

    Article  CAS  PubMed  Google Scholar 

  • Jaswinski AH (1970) Stochastic processes and filtering theory. Academic, New York/London

    Google Scholar 

  • Kaya M, Higuchi H (2010) Nonlinear elasticity and an 8-nm working stroke of single myosin molecules in myofilaments. Science 329:686–689

    Article  CAS  PubMed  Google Scholar 

  • Kitamura K, Tokunaga M, Iwane AH, Yanagida T (1999) A single head moves along an actin filament with regular steps of 5.3 nanometres. Nature 397:129–134

    Article  CAS  PubMed  Google Scholar 

  • Kitamura K, Tokunaga M, Esaki S, Iwane AH, Yanagida T (2005) Mechanism of muscle contraction based on stochastic properties of single actomyosin motors observed in vitro. Biophysics 1:1–19

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Knight AE, Veigel C, Chambers C, Molloy JE (2001) Analysis of single-molecule mechanical recordings: application to actin-myosin interactions. Prog Biophys Mol Biol 77:45–72

    Article  CAS  PubMed  Google Scholar 

  • Kolomeisky AB, Fisher ME (2003) A simple kinetic model describes the processivity of myosin-V. Biophys J 84:1642–1650

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Kron SJ, Spudich JA (1986) Fluorescent actin filaments move on myosin fixed to a glass surface. Proc Natl Acad Sci USA 83:8272–6276

    Article  Google Scholar 

  • Lewalle A, Steffen W, Ouyang Z, Sleep J (2008) Single-molecule measurement of the stiffness of the rigor myosin bond. Biophys J 94:2160–2169

    Article  CAS  PubMed  Google Scholar 

  • Mehta AD, Finer JT, Simmons RM (1997) Detection of snigle molecule interactions using correlated thermal diffusion. Proc Natl Acad Sci USA 94:7927–7931

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Mehta AD, Rock RS, Rief M, Spudich JA, Mooseker MS, Cheney RE (1999) Myosin-V is a processive actin-based motor. Nature 400:590–593

    Article  CAS  PubMed  Google Scholar 

  • Milescu LS, Yildiz A, Selvin PR, Sachs F (2006) Extacting dwell time sequences from processive molecular motor data. Biophys J 91:3135–3150

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Molloy JE, Burns JE, Kendrick-Jones J, Tregear RT, White DCS (1995) Movement and force produced by a single myosin head. Nature 378:209–212

    Article  CAS  PubMed  Google Scholar 

  • Moore JR, Krementsova EB, Trybus KM, Warshaw DM (2004) Does the myosin neck region act as a lever? J Muscle Res Cell Motil 25:28–35

    Article  Google Scholar 

  • Nie C-M, Sasi M, Terada TP (2014) Conformational flexibility of loops of myosin enhances the global bias in the actin-myosin interaction landscape. Phys Chem Chem Phys 16:6441–6447

    Article  CAS  PubMed  Google Scholar 

  • Nishizaka T, Miyata H, Yoshikawa H, Ishiwata S, Kinosita K Jr (1995) Unbinding force of a single motor molecule of muscle studied by optical tweezers. Nature 377:251–254

    Article  CAS  PubMed  Google Scholar 

  • Nishizaka T, Seo R, Tadakuma H, Kinsoita K Jr, Ishiwata S (2000) Characterization of single actomyosin rigor bonds: load dependence of lifetime and mechanical properties. Biophys J 79:962–974

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Page ES (1954) Continuous inspection schemes. Biometrika 41:100–115

    Article  Google Scholar 

  • Patlak JB (1993) Measuring kinetics of complex single ion-channel data using mean-variance histograms. Biophys J 65:29–42

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Piazzesi G, Reconditi M, Linari M, Lucii L, Bianco P, Brunello E, Decostre V, Stewart A, Gore DB, Irving TC, Irving M, Lombardi V (2007) Skeletal muscle performance determined by modulation of number of motors rather than motor force or stroke size. Cell 131:784–795

    Article  CAS  PubMed  Google Scholar 

  • Press WH, Teukolsky SA, Vetterling WT, Flannery BP (1992) Numerical recipes in Fortran, 2nd edn. Cambridge University Press, Cambridge

    Google Scholar 

  • Purcell TJ, Morris C, Spudich JA, Sweeney HL (2002) Role of the lever arm in the processive stepping of myosin V. Proc Natl Acad Sci USA 99:14159–14164

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Rabiner LR (1989) A tutorial on hidden Markov models and selected applications in speech recognition. Proc IEEE 77:257–285

    Article  Google Scholar 

  • Reconditi M, Linari M, Lucii L, Stewart A, Sun YB, Boesecke P, Narayanan T, Fischetti RG, Irving T, Piazzesi G, Irving M, Lombardi V (2004) The myosin motor in muscle generates a smaller and slower working stroke at higher load. Nature 428:578–581

    Article  CAS  PubMed  Google Scholar 

  • Sakamoto T, Wang F, Schmitz S, Xu Y, Molloy JE, Veigel C, Sellers JR (2003) Neck length and processivity of myosin V. J Biol Chem 278:29201–29207

    Article  CAS  PubMed  Google Scholar 

  • Schaller V, Weber C, Semmrich C, Frey S, Bausch AR (2010) Polar patterns of driven filaments. Nature 467:73–77

    Article  CAS  PubMed  Google Scholar 

  • Sellers JR (2000) Myosins: a diverse superfamily. Biochim Biophys Acta 1496:3–22

    Article  CAS  PubMed  Google Scholar 

  • Sleep J, Lewalle A, Smith DA (2006) Reconciling the working strokes of a single head of skeletal muscle myosin estimated from laser-trap experiment and crystal structures. Proc Natl Acad Sci USA 103:1278–1282

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Smith DA (1998a) A quantitative method for the detection of edges in noisy time series. Philos Trans R Soc B 353:1969–1981

    Article  CAS  Google Scholar 

  • Smith DA (1998b) Direct tests of muscle cross-bridge theories: predictions of a Brownian dumbbell model for position-dependent cross-bridge lifetimes and step sizes with an optically trapped actin filament. Biophys J 75:2996–3007

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Smith DA (2004) How processive is the myosin motor? J Muscle Res Cell Motil 25:215–217

    Article  CAS  PubMed  Google Scholar 

  • Smith DA, Steffen W, Simmons RM, Sleep J (2001) Hidden-Markov methods for the analysis of single-molecule actomyosin displacement data: the variance-hidden-Markov method. Biophys J 81:2795–2816

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Steffen W, Smith DA, Simmons RM, Sleep J (2001) Mapping the actin filament with myosin. Proc Natl Acad Sci USA 98:14949–14954

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Stranneby D, Walker W (2004) Digital signal processing and applications, 2nd edn. Elsevier, Amsterdam

    Google Scholar 

  • Sweeney HL, Houdusse A (2004) The motor mechanism of myosin V: insights for muscle contraction. Philos Trans R Soc B 359:1829–1841

    Article  CAS  Google Scholar 

  • Takagi Y, Homsher EE, Goldman YE, Shuman H (2006) Force generation in single conventional actomyosin complexes under high dynamic load. Biophys J 90:1295–1307

    Article  CAS  PubMed  Google Scholar 

  • Takano M, Terada TP, Sasai M (2010) Unidirectional Brownian motion observed in an in silico single molecule experiment of an actomyosin motor. Proc Natl Acad Sci USA 107:7769–7774

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Thomas DD, Ramachandran S, Roopnarine O, Hayuden DW, Ostap EM (1995) The mechanism of force generation in muscle: a disorder-to-order transition, coupled to internal structural changes. Biophys J 68:135s–141s

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Toyoshima YY, Kron SJ, Spudich JA (1990) The myosin step size: measurement of the unit displacement per ATP hydrolyzed in an in vitro assay. Proc Natl Acad Sci USA 87:7130–7134

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Tregear RT, Reedy MC, Goldman YE, Taylor KA, Winkler H, Franzini-Armstrong C, Sasaki H, Lucaveche C, Reedy MK (2004) Cross-bridge number, position and angle in target zones of cryofixed isometrically active insect flight muscle. Biophys J 86:3009–3019

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Tsiavaliaris G, Fujita-Becker S, Manstein DJ (2004) Molecular engineering of a backwards-moving myosin motor. Nature 427:558–561

    Article  CAS  PubMed  Google Scholar 

  • Tyska MJ, Warshaw DM (2002) The myosin power stroke. Cell Motil Cytoskeleton 51:1–15

    Article  CAS  PubMed  Google Scholar 

  • Tyska MJ, Dupuis DFE, Guilford WH, Patlak JH, Waller GS, Trybus KM, Warshaw DM, Lowey S (1999) Two heads are better than one for generating force and motion. Proc Natl Acad Sci USA 96:4402–4407

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Uemura S, Higuchi H, Olivares AO, De La Cruz EM, Ishiwata S (2004) Mechanochemical couping of two substeps in a single myosin V motor. Nat Struct Biol 11:877–883

    Article  CAS  Google Scholar 

  • Uyeda TQP, Kron SJ, Spudich JA (1990) Myosin step size: estimation from slow sliding movement of actin over low densities of heavy meromyosin. J Mol Biol 214:699–710

    Article  CAS  PubMed  Google Scholar 

  • Veigel C, Bartoo ML, White DCS, Sparrow JC, Molloy JE (1998) The stiffness of rabbit skeletal actomyosin cross-bridges determined with an optical tweezers transducer. Biophys J 75:1424–1438

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Veigel C, Coluccio LM, Jontes JD, Sparrow JC, Milligan RA, Molloy JE (1999) The motor protein myosin-I produces its working stroke in two steps. Nature 398:530–533

    Article  CAS  PubMed  Google Scholar 

  • Veigel C, Wang F, Bartoo ML, Sellers JR, Molloy JE (2001) The gated gait of the processive motor, myosin V (2001) Nat Cell Biol 4:59–65

    Article  CAS  Google Scholar 

  • Veigel C, Schmitz S, Wang F, Sellers JR (2005) Load-dependent kinetics of myosin-V can explain its high processivity. Nat Cell Biol 7:861–869

    Article  CAS  PubMed  Google Scholar 

  • Walker M, Zhang X-Z, Jiang W, Trinick J, White HD (1999) Observation of transient disorder during myosin subfragment-1 binding to actin by stopped-flow fluorescence and millisecond time resolution electron cryomicroscopy: evidence that the start of the crossbridge power stroke in muscle has variable geometry. Proc Natl Acad Sci USA 96:465–470

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Walker ML, Burgess SA, Sellers JR, Wang F, Hammer JA III, Trinick J, Knight PJ (2000) Two-headed binding of a processive myosin to F-actin. Nature 405:804–807

    Article  CAS  PubMed  Google Scholar 

  • Warshaw DM, Hayes F, Gaffney D, Lauzon AM, Wu J, Kennedy G, Trybus K, Lowey S, Berger C (1998) Myosin conformational states determined by single fluorophore polarization. Proc Natl Acad Sci USA 95:8034–8039

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Weatherburn CE (1968) A first course in mathematical statistics, 2nd edn. Cambridge University Press, Cambridge

    Google Scholar 

  • Wells AL, Lin AW, Chen LQ, Safter D, Cain SM, Hasson T, Carragher BO, Milligan RA, Sweeney HL (1999) Myosin VI is an actin-based motor that moves backwards. Nature 401:505–508

    Article  CAS  PubMed  Google Scholar 

  • Yanagida T, Arata T, Oosawa F (1985) Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle. Nature 316:366–369

    Article  CAS  PubMed  Google Scholar 

  • Yanagida T, Harada Y, Kodama T (1991) Chemomechanical coupling in actomyosin system: an approach by in vitro movement assay and kinetic analysis of ATP hydrolysis by shortening myofibrils. Adv Biophys 27:237–257

    Article  CAS  PubMed  Google Scholar 

  • Yildiz A, Forkey JN, McKinney SA, Ha T, Goldman YE, Selvin PR (2003) Myosin V walks hand-over-hand: single fluorophore imaging with 1.5nm localization. Science 300:2061–2065

    Article  CAS  PubMed  Google Scholar 

  • Zhao Y, Kawai M (1994) BDM affects nucleotide binding and force generation steps of the crossbridge cycle in rabbit psoas muscle fibers. Am J Phys 266:C437–C447

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Physiology, Anatomy and Microbiology, La Trobe University, Melbourne, VIC, Australia

    David Aitchison Smith

Authors
  1. David Aitchison Smith
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

Copyright information

© 2018 Springer Nature Switzerland AG

About this chapter

Check for updates. Verify currency and authenticity via CrossMark

Cite this chapter

Aitchison Smith, D. (2018). Myosin Motors. In: The Sliding-Filament Theory of Muscle Contraction. Springer, Cham. https://doi.org/10.1007/978-3-030-03526-6_6

Download citation

Publish with us

Policies and ethics

Search

Navigation