KFU. Card publication. Gibbs energies, enthalpies, and entropies of water and lysozyme at the inner edge of excess hydration.

KAZAN
FEDERAL UNIVERSITY

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GIBBS ENERGIES, ENTHALPIES, AND ENTROPIES OF WATER AND LYSOZYME AT THE INNER EDGE OF EXCESS HYDRATION.

Form of presentation

Articles in international journals and collections

Year of publication

2013

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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. Gibbs energies, enthalpies, and entropies of water and lysozyme at the inner edge of excess hydration. / V.A. Sirotkin, A.V. Khadiullina // J. Chem. Phys. – 2013. - Vol. 139. - P. 075102/1-075102/9.

Annotation

The aim of this study is to simultaneously monitor the excess partial Gibbs energies, enthalpies, and entropies of water and white egg lysozyme and demonstrate how these quantities correlate with the coverage of the protein macromolecules by water molecules. Isothermal calorimetry and water sorption measurements were applied to characterize the hydration dependencies of the excess thermodynamic functions. The excess partial quantities are found to be sensitive to changes in the water and protein states. At the lowest water weight fractions (w1), changes in the excess functions are primarily attributable to the addition of water. The transition of lysozyme from a glassy (rigid) to a flexible (elastic) state is accompanied by significant changes in the excess partial quantities. When the charged groups on the protein are covered, this transition occurs at w1 = 0.05; when the coverage of both polar and weakly interacting surface elements is complete, the excess partial quantities become h

Keywords

Lysozyme, enzyme, hydration, Gibbs energy, enthalpy, entropy, water

The name of the journal

J CHEM PHYS

URL

http://scitation.aip.org/content/aip/journal/jcp/139/7/10.1063/1.4818527

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

https://repository.kpfu.ru/eng/?p_id=92572&p_lang=2

Resource files

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Sirotkin_Vladimir_JCP_2013.pdf	1,17	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	2013-01-01T00:00:00Z	ru_RU
dc.date.available	2013-01-01T00:00:00Z	ru_RU
dc.date.issued	2013	ru_RU
dc.identifier.citation	Sirotkin V.A. Gibbs energies, enthalpies, and entropies of water and lysozyme at the inner edge of excess hydration. / V.A. Sirotkin, A.V. Khadiullina // J. Chem. Phys. – 2013. - Vol. 139. - P. 075102/1-075102/9.	ru_RU
dc.identifier.uri	https://repository.kpfu.ru/eng/?p_id=92572&p_lang=2	ru_RU
dc.description.abstract	J CHEM PHYS	ru_RU
dc.description.abstract	The aim of this study is to simultaneously monitor the excess partial Gibbs energies, enthalpies, and entropies of water and white egg lysozyme and demonstrate how these quantities correlate with the coverage of the protein macromolecules by water molecules. Isothermal calorimetry and water sorption measurements were applied to characterize the hydration dependencies of the excess thermodynamic functions. The excess partial quantities are found to be sensitive to changes in the water and protein states. At the lowest water weight fractions (w1), changes in the excess functions are primarily attributable to the addition of water. The transition of lysozyme from a glassy (rigid) to a flexible (elastic) state is accompanied by significant changes in the excess partial quantities. When the charged groups on the protein are covered, this transition occurs at w1 = 0.05; when the coverage of both polar and weakly interacting surface elements is complete, the excess partial quantities become h	ru_RU
dc.language.iso	ru	ru_RU
dc.subject	Lysozyme	ru_RU
dc.subject	enzyme	ru_RU
dc.subject	hydration	ru_RU
dc.subject	Gibbs energy	ru_RU
dc.subject	enthalpy	ru_RU
dc.subject	entropy	ru_RU
dc.subject	water	ru_RU
dc.title	Gibbs energies, enthalpies, and entropies of water and lysozyme at the inner edge of excess hydration.	ru_RU
dc.type	Articles in international journals and collections	ru_RU