New modification of model-free approach to analysis of nuclear magnetic relaxation data in proteins.
A formal approach to the analysis of 13C magnetic relaxation data in proteins has been developed. It is based on the concepts of one of the authors on the internal motions in solid polymers (Fedotov, V.D., Pulse NMR in bulk polymers, Doctoral dissertation, Kazan, USSR, 1981). According to this approach the intermolecular motions in proteins are considered as anisotropic ones and described in terms of a spectrum of correlation times. To characterize the motions a set of formal microdynamic parameters has been introduced. They are: the anisotropy parameter (a measure of spatial restriction of motion), the most probable correlation time, the parameter of the correlation time distribution width. The analysis of protonated carbon relaxation in globular proteins (bovine pancreatic trypsin inhibitor and ribonuclease S) and polymers has been carried out by the model-free approach. Microdynamic parameters of CH3-, CH2-, aromatic CH-groups have been considered within the framework of the diffusional rotation-oscillation models. To explain the backbone CH-group relaxation the model of the defect diffusion has been applied. The distinctive feature of the results obtained is the broad correlation time distribution for all groups of any type. The causes of nonexponential correlation function of local motion have been discussed. To elucidate the nature of the correlation time the carbon magnetization decays in the wide range of microdynamic parameter values imitating various experimental conditions have been calculated.
Fedotov
V D
VD
Institute of Biology, USSR Academy of Sciences, Kazan.
Kivayeva
L S
LS
D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008745:Methylation; D008958:Models, Molecular; D009038:Motion; D010447:Peptide Hydrolases; D012260:Ribonucleases
D012260:Ribonucleases; C022542:ribonuclease S; D010447:Peptide Hydrolases