Laser Raman studies on myosin, C-protein and myosin-C-protein complex.
The Raman spectra of purified myosin, C-protein and myosin-C-protein complex in aqueous solution, as well as that of pelleted filaments, were analyzed. The analyses confirmed that C-protein adopts a predominantly non-alpha-helical structure, while myosin adopts a predominantly alpha-helical structure. Neither 10 mM MgCl2 nor filament formation induced large conformational changes of purified myosin. Thermal denaturation of purified myosin, however, induced large changes in the Raman spectrum owing to conformational changes. It is likely that the binding of myosin and C-protein is not accompanied by large conformational changes of the proteins.
D000818:Animals; D002352:Carrier Proteins; D007834:Lasers; D009124:Muscle Proteins / Q000302:isolation & purification*; D009132:Muscles / Q000032:analysis; D009218:Myosins / Q000302:isolation & purification*; D011485:Protein Binding; D011487:Protein Conformation; D011817:Rabbits; D013059:Spectrum Analysis, Raman; D000099163:Myosin Binding Protein C
D002352:Carrier Proteins; D009124:Muscle Proteins; D009218:Myosins; D000099163:Myosin Binding Protein C