[Nuclear magnetic resonance and intramolecular mobility of proteins].

The quantitative analysis of the data of NMR obtained by different authors in solutions and powders of protein in order to obtain information about the mechanism of intramolecular mobility of macromolecules was. The experiments on selective relaxation 13C and nonselective relaxation 1H in solutions for a number of globular proteins are discussed in detail. Also the experiments on temperature dependences of the broad line spectra of the protons of dry and hydrated proteins are considered. All the experimental data show the absence of the segmental liquid-like motion of the polypeptide chain in the native protein molecule. In the experiments considered only the local anisotropic motions are found which are characteristic of the crystal polymers and related to the torsional vibrations on small angle (15-30 degrees). The only exceptions are the end methyl and methylene groups occupying the periferals of the long side chain, which participate in nearly "free" rotations.