KFU. Card publication. A study of the hydration of ribonuclease A using densitometry: Effect of the protein hydrophobicity and polarity.

KAZAN
FEDERAL UNIVERSITY

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A STUDY OF THE HYDRATION OF RIBONUCLEASE A USING DENSITOMETRY: EFFECT OF THE PROTEIN HYDROPHOBICITY AND POLARITY.

Form of presentation

Articles in international journals and collections

Year of publication

2014

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Authors, employees of KFU

Sirotkin Vladimir Aleksandrovich, author

Authors, students KFU

Khadiullina Aygul Vakilevna, author

Bibliographic description in the original language

Sirotkin, V.A. A study of the hydration of ribonuclease A using densitometry: Effect of the protein hydrophobicity and polarity. / V.A. Sirotkin, A.V. Khadiullina // Chemical Physics Letters. – 2014. – V.603. – P. 13-17.

Annotation

The excess volumes of the binary system of ribonuclease A (RNase A) with water were obtained as a function of composition at 25 ?C. The excess quantities for RNase A were compared with the published data for several unrelated proteins (lysozyme, serum albumin, lactoglobulin, and chymotrypsinogen A). The hydrophobicity of these proteins is gradually changed over a wide range. It was found that the more hydrophilic a protein is, the more significant the hydrophilic hydration contribution is. RNase A is the most hydrophilic protein in the present study, and it has the most significant hydrophilic hydration contribution.

Keywords

Ribonuclease A, volume, water, hydration, hydrophobicity, protein, polarity

The name of the journal

Chemical Physics Letters

URL

http://www.sciencedirect.com/science/article/pii/S0009261414002991

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

https://repository.kpfu.ru/eng/?p_id=92570&p_lang=2

Resource files

File name	Size (MB)	Format
Sirotkin_Vladimir_CPLett_2014.pdf	0,89	pdf	show / download

Full metadata record

Field DC	Value	Language
dc.contributor.author	Sirotkin Vladimir Aleksandrovich	ru_RU
dc.contributor.author	Khadiullina Aygul Vakilevna	ru_RU
dc.date.accessioned	2014-01-01T00:00:00Z	ru_RU
dc.date.available	2014-01-01T00:00:00Z	ru_RU
dc.date.issued	2014	ru_RU
dc.identifier.citation	Sirotkin, V.A. A study of the hydration of ribonuclease A using densitometry: Effect of the protein hydrophobicity and polarity. / V.A. Sirotkin, A.V. Khadiullina // Chemical Physics Letters. – 2014. – V.603. – P. 13-17.	ru_RU
dc.identifier.uri	https://repository.kpfu.ru/eng/?p_id=92570&p_lang=2	ru_RU
dc.description.abstract	Chemical Physics Letters	ru_RU
dc.description.abstract	The excess volumes of the binary system of ribonuclease A (RNase A) with water were obtained as a function of composition at 25 ?C. The excess quantities for RNase A were compared with the published data for several unrelated proteins (lysozyme, serum albumin, lactoglobulin, and chymotrypsinogen A). The hydrophobicity of these proteins is gradually changed over a wide range. It was found that the more hydrophilic a protein is, the more significant the hydrophilic hydration contribution is. RNase A is the most hydrophilic protein in the present study, and it has the most significant hydrophilic hydration contribution.	ru_RU
dc.language.iso	ru	ru_RU
dc.subject	Ribonuclease A	ru_RU
dc.subject	volume	ru_RU
dc.subject	water	ru_RU
dc.subject	hydration	ru_RU
dc.subject	hydrophobicity	ru_RU
dc.subject	protein	ru_RU
dc.subject	polarity	ru_RU
dc.title	A study of the hydration of ribonuclease A using densitometry: Effect of the protein hydrophobicity and polarity.	ru_RU
dc.type	Articles in international journals and collections	ru_RU