KFU. Card publication. Preferential hydration of a-chymotrypsin in acetonitrile: Comparison with FTIR spectroscopy.

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FEDERAL UNIVERSITY

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PREFERENTIAL HYDRATION OF A-CHYMOTRYPSIN IN ACETONITRILE: COMPARISON WITH FTIR SPECTROSCOPY.

Form of presentation

Articles in international journals and collections

Year of publication

2019

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Authors, employees of KFU

Sirotkin Vladimir Aleksandrovich, author

Bibliographic description in the original language

Sirotkin, V.A. Preferential hydration of a-chymotrypsin in acetonitrile: Comparison with FTIR spectroscopy. / 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.57-90.

Annotation

Preferential solvation and hydration of proteins in water-organic mixtures: Two sides of one coin.

Keywords

Preferential hydration, a-chymotrypsin, acetonitrile, FTIR spectroscopy.

The name of the journal

Preferential solvation and hydration of proteins in water-organic mixtures: Two sides of one coin.

URL

https://www.scopus.com/inward/record.uri?eid=2-s2.0-85084275481&partnerID=40&md5=b603c8f11abb363f1985ace6d00f7ed2

Please use this ID to quote from or refer to the card

https://repository.kpfu.ru/eng/?p_id=233977&p_lang=2

Resource files

File name	Size (MB)	Format
Book_2019_Chapter_03.pdf	0,48	pdf	show / download

Full metadata record

Field DC	Value	Language
dc.contributor.author	Sirotkin Vladimir Aleksandrovich	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. Preferential hydration of a-chymotrypsin in acetonitrile: Comparison with FTIR spectroscopy. / 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.57-90.	ru_RU
dc.identifier.uri	https://repository.kpfu.ru/eng/?p_id=233977&p_lang=2	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	The aim of this study is to monitor the preferential hydration of the protein macromolecules at low and high water content in water-organic mixtures. Our approach is based on the analysis of the absolute values of the water/organic solvent sorption. We applied this approach to estimate the protein stabilization/destabilization due to the preferential interactions of -chymotrypsin with water-acetonitrile mixtures. At high water content, proteins are preferentially hydrated. At the intermediate water content, the preferential interaction changed from preferential hydration to preferential binding of acetonitrile. From infrared spectra, changes in the structure of proteins were determined through an analysis of the structure of the amide I band. Acetonitrile augments the intensity of the 1626 cm-1 band assigned to the intermolecular β–sheet aggregates. At low water content, the proteins are in a glassy (rigid) state. The H-bond accepting acetonitrile molecules are not effective in solvating the dehydrated protein molecules alone. Therefore, the acetonitrile molecules are preferentially excluded from the protein surface, resulting in the preferential hydration.	ru_RU
dc.language.iso	ru	ru_RU
dc.subject	Preferential hydration	ru_RU
dc.subject	a-chymotrypsin	ru_RU
dc.subject	acetonitrile	ru_RU
dc.subject	FTIR spectroscopy.	ru_RU
dc.title	Preferential hydration of a-chymotrypsin in acetonitrile: Comparison with FTIR spectroscopy.	ru_RU
dc.type	Articles in international journals and collections	ru_RU