[Interpretation of the pictures of meridional diffraction on X-rays of membrane-free rabbit spinal muscles in a state of rigor and their dependence on physico-chemical parameters of rigorising solution].

Results of the studies of structural and mechanical properties of rabbit psoas muscle by means of X-ray diffraction and physiological technique are summarised along the following lines: localisation of minor proteins in the thick filaments and the origin of meridional reflections in the X-ray diffraction patterns of rigorised rabbit psoas muscle; molecular basis of the effects of pH, ionic strength, pyrophosphate, ethyleneglycol and pyrophosphate-ethyleneglycol mixture on the value of rigor tension and their dependence on the sarcomerès length and concentration of Mg2+; effect of selective extraction of minor proteins from M- and P-zones of the thick filaments on meridional reflections; structure of the thick filaments in the state of "Ca2+-free rigor"; attachment of cross-bridges to actin filaments in relaxing solution (is the model of "sterick brocking" correct?); role of structural transitions in S-2-segments of myosin in force generation.