Форма представления | Статьи в зарубежных журналах и сборниках |
Год публикации | 2019 |
Язык | английский |
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Сироткин Владимир Александрович, автор
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Библиографическое описание на языке оригинала |
Sirotkin, V.A., Kuchierskaya, A.A. Preferential solvation of a-chymotrypsin in water-monohydric alcohol mixtures: Effect of chain lentgth. / In: Sirotkin V.A., (Ed.) Preferential solvation and hydration of proteins in water-organic mixtures: Two sides of one coin. - Nova Science Publishers, Inc., Hauppauge, NY, 2019. - P.25-56. |
Аннотация |
Preferential solvation and hydration of proteins in water-organic mixtures: Two sides of one coin. |
Ключевые слова |
Preferential solvation, of a-chymotrypsin, water, monohydric alcohol |
Название журнала |
Preferential solvation and hydration of proteins in water-organic mixtures: Two sides of one coin.
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URL |
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85084275481&partnerID=40&md5=b603c8f11abb363f1985ace6d00f7ed2 |
Пожалуйста, используйте этот идентификатор, чтобы цитировать или ссылаться на эту карточку |
https://repository.kpfu.ru/?p_id=233976 |
Файлы ресурса | |
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Полная запись метаданных |
Поле DC |
Значение |
Язык |
dc.contributor.author |
Сироткин Владимир Александрович |
ru_RU |
dc.date.accessioned |
2019-01-01T00:00:00Z |
ru_RU |
dc.date.available |
2019-01-01T00:00:00Z |
ru_RU |
dc.date.issued |
2019 |
ru_RU |
dc.identifier.citation |
Sirotkin, V.A., Kuchierskaya, A.A. Preferential solvation of a-chymotrypsin in water-monohydric alcohol mixtures: Effect of chain lentgth. / In: Sirotkin V.A., (Ed.) Preferential solvation and hydration of proteins in water-organic mixtures: Two sides of one coin. - Nova Science Publishers, Inc., Hauppauge, NY, 2019. - P.25-56. |
ru_RU |
dc.identifier.uri |
https://repository.kpfu.ru/?p_id=233976 |
ru_RU |
dc.description.abstract |
Preferential solvation and hydration of proteins in water-organic mixtures: Two sides of one coin. |
ru_RU |
dc.description.abstract |
Preferential solvation and hydration of bovine pancreatic α-chymotrypsin was investigated in the entire range of water content in monohydric alcohols at 25?C. This approach is based on the analysis of absolute values of the water and monohydric alcohol sorption. One of the most important advantages of our approach is the facilitation of individual evaluation of the Gibbs energies of water, alcohol, and protein in the entire range of water content. This methodology was applied to estimate protein destabilization/stabilization of lysozyme in water-monohydric alcohol mixtures.
Three distinct schemes are operative in water-alcohol mixtures. α-chymotrypsin is preferentially hydrated at high water content. Protein has a higher affinity for alcohol than for water at intermediate water content. At low water content, preferential solvation of chymotrypsin depends significantly on the alkyl chain length. Opposite to methanol, ethanol and propanol-1 are preferentially excluded from the protein surface at the lowest water content. This results in preferential hydration of α-chymotrypsin in the water-poor ethanol and propanol-1. Our data clearly show that the length of the alkyl chain of monohydric alcohols is one of the critical factors in determining the stability of protein-water-alcohol systems.
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ru_RU |
dc.language.iso |
ru |
ru_RU |
dc.subject |
Preferential solvation |
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dc.subject |
of a-chymotrypsin |
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dc.subject |
water |
ru_RU |
dc.subject |
monohydric alcohol |
ru_RU |
dc.title |
Preferential solvation of a-chymotrypsin in water-monohydric alcohol mixtures: Effect of chain lentgth. |
ru_RU |
dc.type |
Статьи в зарубежных журналах и сборниках |
ru_RU |
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