Abstract
The concentration dependences of self-diffusion coefficient for irregular-shaped fibrinogen, for globular, spheroidal trypsin and α-chymotrypsin were studied by pulsed field gradient nuclear magnetic resonance. The experimental data were analyzed in a view of two known theoretical approaches—the hydrodynamic model of rigid spheres by Tokuyama and Oppenheim and the phenomenological approach based on the frictional formalism of non-equilibrium thermodynamics by Vink. The detailed discussion of their merits and drawbacks is presented. Our results testify that the Vink’s approach is quite universal, providing a satisfactory description of experimental data for proteins of complicated structure and different shape while the model of Tokuyama and Oppenheim is applicable only to proteins of more regular shape.
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Acknowledgements
We thank Dr. D. Faizullin (Kazan Institute of Biochemistry and Biophysics, Russian Federation) for helpful suggestions on the structure of studied proteins, Dr. R. Litvinov (University of Pennsylvania, USA), Dr. A. Zhmurov and Dr. V. Barsegov (Moscow Institute of Physics and Technology, Russian Federation) for helpful discussion about self-diffusion of fibrinogen. This work was supported by grants from the Russian Foundation for Basic Research and the Government of Tatarstan Republic (no. 15-44-02230) and from the Russian Foundation for Basic Research (no. 15-29-01239). Part of the work was performed in accordance with the Russian Government Program of Competitive Growth of Kazan Federal University.
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Kusova, A.M., Sitnitsky, A.E., Idiyatullin, B.Z. et al. The Effect of Shape and Concentration on Translational Diffusion of Proteins Measured by PFG NMR. Appl Magn Reson 49, 35–51 (2018). https://doi.org/10.1007/s00723-017-0957-y
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DOI: https://doi.org/10.1007/s00723-017-0957-y