Proceedings of the Royal Society of London. Series B, Biological sciences · 1953 · 190 citations · 0 references
Life SciencesBiochemistryBiophysicsCytoskeletonProtein BiochemistryStructural BiologyMuscle MechanicsMuscle PhysiologyMuscle StructureProtein StructureX-ray CrystallographyX-ray DiffractionActin Atp HydrolysisActin-myosin ContractilityEnergyMolecular Structure DeterminationMuscle Contractile FunctionMyosin Atp HydrolysisMyosin BiochemistryX-ray Diffraction Analysis
Abstract The present-day picture of muscle is briefly as follows: muscle is a machine for converting chemical energy into mechanical work; the ‘moving parts’ of this machine are built up of two proteins, actin and myosin; the known energy-producing reaction most closely linked to the contractile process is the dephosphorylation of adenosine triphosphate (ATP). In the present studies, low-angle X-ray diffraction technique has been used to study the molecular structure of these two proteins, actin and myosin, and their arrangement in living muscle under various conditions.