In muscle, work is performed by myosin cross-bridges during interactions wi
th actin filaments. The amount of work performed during each interaction ca
n be related to the mechanical properties of the cross-bridge; work is the
integral of the force produced with respect to the distance that the cross-
bridge moves the actin filament, anal force is determined by the stiffness
of the attached cross-bridge. In this paper, cross-bridge stiffness in frog
sartorius muscle was estimated from thermodynamic efficiency (work/free en
ergy change) using a two-state cross-bridge model, assuming constant stiffn
ess over the working range and tight-coupling between cross-bridge cycles a
nd ATP use. This model accurately predicts mechanical efficiency (work/enth
alpy output). A critical review of the literature indicates that a realisti
c value for maximum thermodynamic efficiency of frog sartorius is 0.45 unde
r conditions commonly used in experiments on isolated muscle. Cross-bridge
stiffness was estimated for a range of power stroke amplitudes. For realist
ic amplitudes (10-15 nm), estimated cross-bridge stiffness was between 1 an
d 2.2 pN nm(-1). These values are similar to those estimated from quick-rel
ease experiments, taking into account compliance arising from structures ot
her than cross-bridges, but are substantially higher than those from isolat
ed protein studies. The effects on stiffness estimates of relaxing the tigh
t-coupling requirement and of incorporating more force-producing cross-brid
ge states are also considered. (C) Kluwer Academic Publishers.