The mechanics of the actomyosin interaction have been extensively studied using the
organized filament array of striated muscle. However, the extrapolation of these data to the …

Myosin is an ATPase that converts chemical energy into directed movement and can be
viewed as a molecular motor. This protein comes in many shapes and sizes. Over 11 …

The structure of the vanadate-trapped ADP complex of a truncated head of Dictyostelium
myosin II consisting of residues Asp 2− Asn 762 has been determined by molecular …

The effect of temperature on elementary steps of the cross-bridge cycle was investigated
with sinusoidal analysis technique in skinned rabbit psoas fibers. We studied the effect of …

To investigate the kinetic parameters of the crossbridge cycle that regulate force and
shortening in cardiac muscle, we compared the mechanical properties of cardiac trabeculae …

The mechanical behavior of skinned rabbit psoas muscle fiber contractions and in vitro
motility of F-actin (V f) have been examined using ATP, CTP, UTP, or their 2-deoxy forms …

Active glycerinated rabbit psoas fibers were stretched at constant velocity (0.1–3.0 lengths/s)
under sarcomere length control. As observed by previous investigators, force rose in two …

The relation between the chemical and mechanical steps of the myosin-actin ATPase
reaction that leads to generation of isometric force in fast skeletal muscle was investigated in …

In striated muscle thin filament activation is initiated by Ca 2+ binding to troponin C and
augmented by strong myosin binding to actin (cross-bridge formation). Several lines of …

Fatigue of skeletal muscle involves many systems beginning with the central nervous system
and ending with the contractile machinery. This review concentrates on those factors that …