Form of presentation | Articles in international journals and collections |
Year of publication | 2015 |
Язык | английский |
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Khayrutdinov Bulat Imamutdinovich, author
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Ermakova Elena Andreevna, author
Nesmelova Irina Vyacheslavovna, author
Zuev Yuriy Fedorovich, author
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Bibliographic description in the original language |
Herring C.A. Dynamics and thermodynamic properties of CXCL7 chemokine [Tekst] / Charles A. Herring, Christopher M. Singer1, Elena A. Ermakova, Bulat I. Khairutdinov, Yuriy F. Zuev, Donald J. Jacobs and Irina V. Nesmelova // Proteins: Structure, Function, and Bioinformatics. – 2015. Vol. 83. – P. 1987-2007 |
Annotation |
Chemokines form a family of signaling proteins mainly responsible for directing the traffic of leukocytes, where their biological activity can be modulated by their oligomerization state. We characterize the dynamics and thermodynamic stability of monomer and homodimer structures of CXCL7, one of the most abundant platelet chemokines, using experimental methods that include circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy, and computational methods that include the anisotropic network model (ANM), molecular dynamics (MD) simulations and the distance constraint model (DCM). A consistent picture emerges for the effects of dimerization and Cys5-Cys31 and Cys7-Cys47 disulfide bonds formation. The presence of disulfide bonds is not critical for maintaining structural stability in the monomer or dimer, but the monomer is destabilized more than the dimer upon removal of disulfide bonds. Disulfide bonds play a key role in shaping the characteristics of native state dyn |
Keywords |
chemokine; CXCL7; dimer; thermal unfolding; CD spectroscopy; disulfide bonds; distance constraint model; dynamics |
The name of the journal |
Proteins: Structure, Function, and Bioinformatics
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On-line resource for training course |
http://dspace.kpfu.ru/xmlui/bitstream/handle/net/32500/2015_prot24913.pdf?sequence=1&isAllowed=y
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URL |
http://onlinelibrary.wiley.com/doi/10.1002/prot.24913/full |
Please use this ID to quote from or refer to the card |
https://repository.kpfu.ru/eng/?p_id=120284&p_lang=2 |
Resource files | |
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Full metadata record ![](https://shelly.kpfu.ru/pdf/picture/arrow_black_right.gif) |
Field DC |
Value |
Language |
dc.contributor.author |
Khayrutdinov Bulat Imamutdinovich |
ru_RU |
dc.contributor.author |
Ermakova Elena Andreevna |
ru_RU |
dc.contributor.author |
Nesmelova Irina Vyacheslavovna |
ru_RU |
dc.contributor.author |
Zuev Yuriy Fedorovich |
ru_RU |
dc.date.accessioned |
2015-01-01T00:00:00Z |
ru_RU |
dc.date.available |
2015-01-01T00:00:00Z |
ru_RU |
dc.date.issued |
2015 |
ru_RU |
dc.identifier.citation |
Herring C.А. Dynamics and thermodynamic properties of CXCL7 chemokine [Текст] / Charles A. Herring, Christopher M. Singer1, Elena A. Ermakova, Bulat I. Khairutdinov, Yuriy F. Zuev, Donald J. Jacobs and Irina V. Nesmelova // Proteins: Structure, Function, and Bioinformatics. – 2015. Vol. 83. – P. 1987-2007 |
ru_RU |
dc.identifier.uri |
https://repository.kpfu.ru/eng/?p_id=120284&p_lang=2 |
ru_RU |
dc.description.abstract |
Proteins: Structure, Function, and Bioinformatics |
ru_RU |
dc.description.abstract |
Chemokines form a family of signaling proteins mainly responsible for directing the traffic of leukocytes, where their biological activity can be modulated by their oligomerization state. We characterize the dynamics and thermodynamic stability of monomer and homodimer structures of CXCL7, one of the most abundant platelet chemokines, using experimental methods that include circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy, and computational methods that include the anisotropic network model (ANM), molecular dynamics (MD) simulations and the distance constraint model (DCM). A consistent picture emerges for the effects of dimerization and Cys5-Cys31 and Cys7-Cys47 disulfide bonds formation. The presence of disulfide bonds is not critical for maintaining structural stability in the monomer or dimer, but the monomer is destabilized more than the dimer upon removal of disulfide bonds. Disulfide bonds play a key role in shaping the characteristics of native state dyn |
ru_RU |
dc.language.iso |
ru |
ru_RU |
dc.subject |
|
ru_RU |
dc.title |
Dynamics and thermodynamic properties of CXCL7 chemokine |
ru_RU |
dc.type |
Articles in international journals and collections |
ru_RU |
|