Biopolymers and cell. 1987. Volume 3. № 4. 178 - 187

V. D. Fedotov, L. S. Kivaeva

ANALYSIS OF DATA ON MAGNETIC RELAXATION OF 13C NUCLEI IN GLOBULAR PROTEINS

Summary

    Protonated carbons' relaxation in bovine pancreatic trypsin inhibitor and ribonuclease S has been analyzed by the model-free approach based on ideology of relaxation treatment in solid polymers. Microdynamic parameters of CH3-, CH2-, aromatic CH-groups (anisotropy parameters, the most probable correlation times) are considered within the diffusion rotation-oscillation models. A model of the defect diffusion is applied to explain the backbone CH-group relaxation. A distinctive feature of the results obtained is that wide correlation time distributions are found for groups of all the types. Decays of the carbon magnetization in the wide range of microdynamic parameter values imitating the various experimental conditions are calculated to elucidate a nature of the correlation time spectra.