[The effect of electrostatic intermolecular interactions on Brownian rotation of proteins in solution].
A qualitative model that takes into account the influence of electrostatic interactions on the form of correlation function of Brownian rotation of a protein as a whole is given. It is supposed that these interactions give rise to anisotropy of Brownian rotation and this leads to the nonexponentiality of the correlation function. To define experimentally the form of the correlation function nonselective measurements of relaxation times T1 and T2 of protein protons at different resonance frequencies in lysozyme solution were carried out. Literature data on frequency dependencies of relaxation time T1 of water in protein solutions were analysed. Analysis of experiments confirms the proposed model. Correlation times, activation energies and parameters of anisotropy were found.
Krushel'nitskiĭ
A G
AG
Fedotov
V D
VD
D016880:Anisotropy; D004560:Electricity; D009113:Muramidase / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D012996:Solutions
D011506:Proteins; D012996:Solutions; D009113:Muramidase
Vliianie élektrostaticheskikh mezhmolekuliarnykh vzaimodeĭstviĭ na Brounovskoe vrashchenie belkov v rastvore.