[Role of conformational lability in the hydrolysis of ATP by myosin].
Melting temperature of myosin Tm against the concentration of D2O in the system was studied. The D2O/Tm relationship is analogous to that between the kinetics isotope effect and the volumic fraction of D2O in the system. This similarity as well as the difference between the observed kinetic and thermodynamic isotopic effects and the theoretical ones make us suggest that the conformational changes in myosin during ATP hydrolysis are rather substantial.
D000255:Adenosine Triphosphate; D002384:Catalysis; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D008968:Molecular Conformation; D009218:Myosins; D013816:Thermodynamics
D000255:Adenosine Triphosphate; D009218:Myosins
Rol' konformatsionnoĭ podvizhnosti v reaktsii gidroliza ATF miozinom.