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α-chymotrypsin in water–acetone and water–dimethyl sulfoxide mixtures: Effect of preferential solvation and hydration

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dc.contributor.author Sirotkin V.
dc.contributor.author Kuchierskaya A.
dc.date.accessioned 2018-04-05T07:09:24Z
dc.date.available 2018-04-05T07:09:24Z
dc.date.issued 2017
dc.identifier.issn 0887-3585
dc.identifier.uri http://dspace.kpfu.ru/xmlui/handle/net/129715
dc.description.abstract © 2017 Wiley Periodicals, Inc. We investigated water/organic solvent sorption and residual enzyme activity to simultaneously monitor preferential solvation/hydration of protein macromolecules in the entire range of water content at 25°C. We applied this approach to estimate protein destabilization/stabilization due to the preferential interactions of bovine pancreatic α-chymotrypsin with water-acetone (moderate-strength H-bond acceptor) and water-DMSO (strong H-bond acceptor) mixtures. There are three concentration regimes for the dried α-chymotrypsin. α-Chymotrypsin is preferentially hydrated at high water content. The residual enzyme activity values are close to 100%. At intermediate water content, the dehydrated α-chymotrypsin has a higher affinity for acetone/DMSO than for water. Residual enzyme activity is minimal in this concentration range. The acetone/DMSO molecules are preferentially excluded from the protein surface at the lowest water content, resulting in preferential hydration. The residual catalytic activity in the water-poor acetone is ∼80%, compared with that observed after incubation in pure water. This effect is very small for the water-poor DMSO. Two different schemes are operative for the hydrated enzyme. At high and intermediate water content, α-chymotrypsin exhibits preferential hydration. However, at intermediate water content, in contrast to the dried enzyme, the initially hydrated α-chymotrypsin possesses increased preferential hydration parameters. At low water content, no residual enzyme activity was observed. Preferential binding of DMSO/acetone to α-chymotrypsin was detected. Our data clearly demonstrate that the hydrogen bond accepting ability of organic solvents and the protein hydration level constitute key factors in determining the stability of protein–water–organic solvent systems.
dc.relation.ispartofseries Proteins: Structure, Function and Bioinformatics
dc.subject bovine pancreatic α-chymotrypsin
dc.subject dimethyl sulfoxide (DMSO)
dc.subject preferential solvation
dc.subject protein hydration
dc.subject protein stabilization
dc.title α-chymotrypsin in water–acetone and water–dimethyl sulfoxide mixtures: Effect of preferential solvation and hydration
dc.type Article
dc.relation.ispartofseries-issue 10
dc.relation.ispartofseries-volume 85
dc.collection Публикации сотрудников КФУ
dc.relation.startpage 1808
dc.source.id SCOPUS08873585-2017-85-10-SID85021382833


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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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