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Interaction between DNA and chromosomal proteins HMGB1 and H1 studied by IR/VCD spectroscopyстатья
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: 4 апреля 2017 г.
- Авторы: Polyanichko A.M., Chikhirzhina E.V.
- Журнал: Journal of Molecular Structure
- Том: 1044
- Год издания: 2013
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 167
- Последняя страница: 172
- DOI: 10.1016/j.molstruc.2013.01.073
- Аннотация: Binary complexes of calf thymus DNA with calf thymus non-histone chromosomal protein HMGB1 and linker histone H1 were studied using FTIR/VCD spectroscopy. The spectroscopic data showed that the interaction of the protein HMGB1 and histone H1 with DNA resulted in formation of two different types of the macromolecular complexes. Histone H1 retained its native structure even at high concentrations and induced DNA condensation upon binding at the protein to DNA ratio r (w/w) in the complex rP0.3. HMGB1 demonstrated the ability to form soluble complexes at considerably higher protein to DNA ratios. The obtained data suggest that the HMGB1 also participated in the protein–protein interactionsvia its C-terminal domain.
- Добавил в систему: Чихиржина Елена Всеволодовна