In pioneering studies on the 31P NMR spectra of MgADP bound to the "molecular motor" myosin subfragment 1 (S1) in the temperature range of 0 to 25 degrees C, Shriver and Sykes [Biochemistry 20 (1981) 2004-2012/6357-6362; Biochemistry 21 (1982) 3022-3028], proposed that MgADP binds to myosin S1 as a mixture of two interconvertible conformers with different chemical shifts for the beta-P resonance of the S1-bound MgADP and that the concentrations of these conformers are related by an equilibrium constant K(T). Their model implied that the weighted average of the chemical shifts of the beta-P(MgADP) for S1-bound MgADP asymptotically approaches a high temperature limit. Here, and in our earlier paper [K. Konno, K. Ue, M. Khoroshev, H., Martinez, B.D. Ray, M.F. Morales, Proc. Natl. Acad. Sci. USA 97 (2000) 1461-1466], we report experimental similarities to Shriver and Sykes, but diverge from them (especially at 0 degrees C) in not finding two distinct peaks and in finding that the average chemical shift does not change with temperature. Our observations can be explained by chemical exchange of beta-P(MgADP) of S1-bound MgADP between two nearly energetically equivalent environments.
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