The cross-bridge cycle for actin, S1 myosin, and nucleotides in solution is applied to the sliding filament model for fully activated striated muscle. The cycle has attached and rotated isomers of each actomyosin state. It is assumed that these forms have different zero-strain conformations with respect to the filament and that strain-free rate constants are the nominal solution values. Only one S1 unit of heavy meromyosin is considered. Transition-state theory is used to predict the strain dependences of S1 binding to actin, the force-generating transition to rotated states, and the release/binding of nucleotide and phosphate. We propose that ADP release and ATP binding are blocked by positive strain and phosphate release by negative strain. At large strains, rapid dissociation of S1 nucleotide from actin is expected when the compliant element of the cross-bridge is strained in either direction beyond its elastic limits. The dynamical behavior of this model of muscle contraction is discussed in general terms. Its computed steady-state properties are presented in an accompanying paper. © 1995, The Biophysical Society. All rights reserved.
Smith, D. A., & Geeves, M. A. (1995). Strain-dependent cross-bridge cycle for muscle. Biophysical Journal, 69(2), 524–537. https://doi.org/10.1016/S0006-3495(95)79926-X