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pH-induced changes of the structure of small heat shock proteins with molecular mass 24/27 kDa (HspB1)статья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: Chernik I.S., Panasenko O.O., Li Y., Marston S.B., Gusev N.B.
- Журнал: Biochemical and Biophysical Research Communications
- Том: 324
- Номер: 4
- Год издания: 2004
- Издательство: Academic Press
- Местоположение издательства: United States
- Первая страница: 1199
- Последняя страница: 1203
- DOI: 10.1016/j.bbrc.2004.09.176
- Аннотация: The effect of pH on the structure of recombinant chicken Hsp24, human Hsp27 and their 3D mutants mimicking phosphorylation ;at Ser15, Ser77/78, and Ser81/82 was analyzed. Circular dichroism and fluorescent spectroscopy indicate that changes of pH in the range 6.0-7.5 weakly affected the secondary and tertiary structure of the wild type proteins, but induced noticeable changes in the structure of their 3D mutants. According to size-exclusion chromatography and analytical ultracentrifugation variation of pH-induced pronounced changes in the quaternary structure of small heat shock proteins and acidification resulted in accumulation of large oligomers of Hsp24/27. It is concluded that small changes of pH strongly affect the quaternary structure of small heat shock proteins and by this means can influence their functioning in the cell. (C) 2004 Elsevier Inc. All rights reserved.
- Добавил в систему: Гусев Николай Борисович