An electron spin resonance study of temperature-induced structural changes of the spin-labeled myosin head: an evidence for two conformational states of myosin head.
Heavy meromyosin labeled at the SH1 thiol group with an iodoacetamide spin label was studied by electron spin resonance spectroscopy at various temperatures in the presence and absence of nucleotides and PPi. The electron spin resonance spectra of the spin label bound to myosin head showed temperature-dependent changes indicating changes of the structure around the SH1 thiol group of the myosin head. As the temperature was elevated, the bound spin label was more mobilized in all the systems examined. The mobilization of the bound spin label by the elevation of temperature was enhanced in the presence of nucleotides or PPi. The temperature-dependent spectral changes had isosbestic points indicating that the structural changes around the SH1 thiol group took place between two states of the bound spin label, a weakly immobilized and a strongly immobilized state.
D000818:Animals; D004578:Electron Spin Resonance Spectroscopy; D007460:Iodoacetamide; D015879:Myosin Subfragments; D009218:Myosins; D011485:Protein Binding; D011487:Protein Conformation; D011817:Rabbits; D013696:Temperature
D015879:Myosin Subfragments; D009218:Myosins; D007460:Iodoacetamide