A SEARCH FOR PROTEIN STRUCTURAL-CHANGES ACCOMPANYING THE CONTRACTILE INTERACTION

It appears that small movements (detected hitherto only by fluorescence resonance energy transfer measurements and crosslinking studies) in a region of the myosin S-1 particle may mediate chemomechanical energy transduction in the contractile system. Here we find under conditions of high precision at 10-degrees-C and 20-degrees-C that ATP binding to S-1 causes small (0.4%) changes in CD signal, DELTA-epsilon-222, as do temperature changes in the regime below 16-degrees-C. ATP binding perturbs tryptophan residues that we now think are in the mobile region, and we find here that temperature affects tryptophan fluorescence in much the same way that it affects the CD signal, so we believe that the CD signal reports transduction-related movements in S-1. If S-1 is exposed to the range 16-30-degrees-C, CD signal falls with temperature; ATP counteracts this fall. Analysis of vacuum-UV CD spectra yields 42% alpha-helix, 9% antiparallel beta-sheet, 7% parallel beta-sheet, 14% beta-turns, and 29% other structures.