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Abstract
During ATP hydrolysis by spin‐labelled myosin the time‐dependent local conformational changes near S1 thiol groups have been observed. In the steady‐state stage of ATP hydrolysis practically all myosin molecules are in conformationally changed state M̃. After reaction, part of the myosin molecules returns to the initial conformational state M, and another part remains in conformation M̃ forming a complex with ADP.
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