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Protein translational diffusion and intermolecular interactions of globular and intrinsically unstructured proteins

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dc.contributor.author Kusova A.
dc.contributor.author Sitnitsky A.
dc.contributor.author Faizullin D.
dc.contributor.author Zuev Y.
dc.date.accessioned 2020-01-15T21:46:13Z
dc.date.available 2020-01-15T21:46:13Z
dc.date.issued 2019
dc.identifier.issn 1089-5639
dc.identifier.uri https://dspace.kpfu.ru/xmlui/handle/net/155783
dc.description.abstract Copyright © 2019 American Chemical Society. The study of intermolecular interactions of proteins has been an important problem for many years. This paper presents an approach to analyze different levels of protein interactions in solutions through a set of the second- A nd higher-order virial coefficients. The proposed approach is based on the diversified analysis of protein translational collective diffusion and self-diffusion obtained by dynamic light scattering and the pulsed-field gradient NMR (PFG NMR) spectroscopy experimental data. The experimental results were analyzed within the theoretical approach based on Vink's frictional formalism of nonequilibrium thermodynamics and the standard Derjaguin-Landau-Verwey-Overbeekb (DLVO) theory of interactions of colloid particles in electrolyte solutions. The second- A nd higher-order virial coefficients were obtained to estimate the pairwise and many-body intermolecular interactions in the solutions of globular α-chymotrypsin and intrinsically unstructured αS-casein. The second virial coefficients were calculated from the model of the protein-protein potential of mean force. The description of protein-protein interactions includes a set of interaction potentials: The attractive charge-dipole, dipole-dipole, the dispersion Hamaker, the mean force osmotic-attraction, and the repulsive charge-charge ones. It has been found that the major contribution to the intermolecular αS-casein interactions is made by the repulsive charge-charge potential, whereas for the case of α-chymotrypsin, the contributions from other types of interaction are of importance. It was determined that the model was well suited to describe the interactions of both globular and intrinsically disordered proteins. The suggested combination of Vink's approach and the DLVO theory is novel and holds much promise to make a profound analysis of the processes in systems containing various types of protein molecules. ©
dc.relation.ispartofseries Journal of Physical Chemistry A
dc.title Protein translational diffusion and intermolecular interactions of globular and intrinsically unstructured proteins
dc.type Article
dc.collection Публикации сотрудников КФУ
dc.source.id SCOPUS10895639-2019-SID85074891130


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  • Публикации сотрудников КФУ Scopus [24551]
    Коллекция содержит публикации сотрудников Казанского федерального (до 2010 года Казанского государственного) университета, проиндексированные в БД Scopus, начиная с 1970г.

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