[Study of the conformational mobility of globular proteins in aqueous solutions according to their proton relaxation in a rotating system of coordinates].

Measurements of the nuclear magnetization decay in the rotating frame for protons of SA and RNAase proteins in aqueous solutions indicate the dispersion of the relaxation rate for SA protons within the region of correlation frequencies of 10(5)--10(6) s-1. These frequencies are much lower than frequencies of rotational diffusion movements of the SA macromolecules in aqueous solutions. These must be ascribed to internal movement within protein globules due to which the distances between interacting magnetic moments are changed. This conclusion gives direct evidence in favour of existence of conformational mobility in most of the protein globule volume.