The review summarizes the results of studies on conformational changes in contractile proteins that occur during muscle contraction. Polarized fluorescence of tryptophan residues in actin and of fluorescent probes bound specifically to different sites on actin, myosin, or tropomyosin in muscle fibers was measured. The results show that the transition of actomyosin complex from the weak to the strong-binding state is accompanied by a change in the orientation of F-actin subunits with the C and N termini moving opposite to a large part of the subunit. Myosin light chains and some areas in the 20-kDa domain of myosin head move in the same direction as the C- and N-terminal regions of actin. It is established that troponin, caldesmon, calponin, and myosin systems of regulation of muscle contraction modify intramolecular actomyosin rearrangements in a Ca(2+)-dependent manner. The role of intramolecular movements of contractile proteins in muscle contraction is discussed.