
It has recently been reported that tropomyosin exists exclusively as a dimer in physiological salt conditions. It is shown in the present work using analytical ultracentrifugation that, on the contrary, tropomyosin is in equilibrium between monomer, dimer and tetramer with a weak tendency to dimerize and tetramerize. Such a finding has consequences for the assembly of the tropomyosin–actin complex.
Temperature, Tropomyosin, Hydrogen-Ion Concentration, Polymerization, Solutions, Kinetics, Analytical ultracentrifugation, Muscle, Animals, Thermodynamics, Rabbits, Ultracentrifugation, Actin, Protein Binding
Temperature, Tropomyosin, Hydrogen-Ion Concentration, Polymerization, Solutions, Kinetics, Analytical ultracentrifugation, Muscle, Animals, Thermodynamics, Rabbits, Ultracentrifugation, Actin, Protein Binding
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