The concentration dependences of self-diffusion coefficient of various proteins: fibrinogen, trypsin, α-chymotrypsin and αS-casein were studied by means of the pulse field gradient nuclear magnetic resonance. The experimental data was analyzed in a view of the Vink’s phenomenological approach based on the frictional formalism of non-equilibrium thermodynamics. The obtained results indicate that the phenomenological approach is universal and provides an adequate description of the experimental data for proteins of different structure and shape in a wide concentration range. With the help of Vink’s approach the diffusion mobility of proteins was characterized. The concentration was determined, when the αS-casein oligomerization appears.
87.15.kr Protein-solvent interactions
82.56.Pp NMR of biomolecules
$^1$Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center of RAS, Russian Federation\
$^2$Kazan Federal University
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