[Collagen structure and the disordering of the water subsystem in fibrillar polypeptides according to 2H-NMR data].

2H NMR spectra of native collagen of rat tail tendon doped by 2H2O were studied. It was shown that the fine structure of 2H NMR multicomponent spectra is related to the diffusion mobility of constituent water molecules and their partial ordering. A bimodality of the distribution of the H2O ordering parameter was revealed, which corresponds to the alternation of dense and loose regions in the supramolecular structure of collagen-type polypeptides. The lower values of the ordering parameter correspond to loose regions of the structure characterized by the cooperative dynamics of polypeptide chains and water molecules.