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The Effect of Shape and Concentration on Translational Diffusion of Proteins Measured by PFG NMR

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dc.date.accessioned 2019-01-22T20:38:41Z
dc.date.available 2019-01-22T20:38:41Z
dc.date.issued 2018
dc.identifier.issn 0937-9347
dc.identifier.uri https://dspace.kpfu.ru/xmlui/handle/net/148098
dc.description.abstract © 2017, Springer-Verlag GmbH Austria. 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.
dc.relation.ispartofseries Applied Magnetic Resonance
dc.title The Effect of Shape and Concentration on Translational Diffusion of Proteins Measured by PFG NMR
dc.type Article
dc.relation.ispartofseries-issue 1
dc.relation.ispartofseries-volume 49
dc.collection Публикации сотрудников КФУ
dc.relation.startpage 35
dc.source.id SCOPUS09379347-2018-49-1-SID85029738145


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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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