title: Evaluation of the sliding distance in shortening muscles and in polymerizing actin from Hill's force-velocity equation.
abstract: The relationship derived earlier between the sliding distance, Deltal(m), and a/P(0), the characteristic parameter of Hill's force-velocity equation for muscle contraction, was re-formulated in order to get a more general relationship which can be applied also to other biological mechano-chemical energy converters: alpha x Deltal(m)=phi (0)(a/P(0))Deltal(m)=-Deltag where Deltag is the free energy change accompanying the hydrolysis of one ATP molecule while alpha and phi (0) are, respectively, the average forces developed by a myosin head-actin complex which are responsible for shortening and for isometric tension generation. These two molecular forces are different in magnitude and in nature and it is demonstrated that alpha , not phi (0), is the true contractile force. The values of alpha and of phi (0) have been calculated for three muscles. The equation has been successfully applied to actin polymerization-based motility. The value of Deltag in different muscles under different environmental conditions can be easily determined from this equation with the value of Deltal(m) derived experimentally.
authors.affiliation: Department of Structural Biology, The Weizmann Institute of Science, Rehovot 76100, Israel. avraham.oplatka@weizmann.ac.il
authors.forename: Avraham
authors.initials: A
authors.lastname: Oplatka
mesh_terms: D000199:Actins / Q000737:chemistry / Q000502:physiology*; D001696:Biomechanical Phenomena; D001704:Biopolymers / Q000737:chemistry / Q000502:physiology; D006801:Humans; D008954:Models, Biological; D046912:Multiprotein Complexes; D009119:Muscle Contraction / Q000502:physiology*; D018482:Muscle, Skeletal / Q000737:chemistry / Q000502:physiology; D013816:Thermodynamics
chemical_list: D000199:Actins; D001704:Biopolymers; D046912:Multiprotein Complexes