A study of the hydration of ribonuclease A using densitometry: Effect of the protein hydrophobicity and polarity

dc.contributor.author	Sirotkin V.
dc.contributor.author	Khadiullina A.
dc.date.accessioned	2018-09-18T20:02:36Z
dc.date.available	2018-09-18T20:02:36Z
dc.date.issued	2014
dc.identifier.issn	0009-2614
dc.identifier.uri	https://dspace.kpfu.ru/xmlui/handle/net/136008
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. © 2014 Elsevier B.V. All rights reserved.
dc.relation.ispartofseries	Chemical Physics Letters
dc.title	A study of the hydration of ribonuclease A using densitometry: Effect of the protein hydrophobicity and polarity
dc.type	Article
dc.relation.ispartofseries-volume	603
dc.collection	Публикации сотрудников КФУ
dc.relation.startpage	13
dc.source.id	SCOPUS00092614-2014-603-SID84900463445

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