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Conformation of gramicidin A in Triton X-100 micelles from CD and FTIR data: a clean example of antiparallel double β5.6 helix formationстатья
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: 1 августа 2016 г.
- Авторы: Sychev S.V., Barsukov L.I., Ivanov V.T.
- Журнал: Journal of Peptide Science
- Том: 19
- Номер: 7
- Год издания: 2013
- Издательство: John Wiley & Sons Inc.
- Местоположение издательства: United States
- Первая страница: 452
- Последняя страница: 458
- DOI: 10.1002/psc.2519.
- Аннотация: The linear peptide gramicidin A (gA) forms prototypical ion channels specific for monovalent cations and has been extensively used to study the organization and dynamics of membrane channels. This polymorphic peptide can adopt two different types of structures, the helical dimer β6.3 ('channel state') and the double helical structure with two intertwined monomers. The structure of gA in micelles of detergent Triton X-100 has been studied using CD, Fourier transform infrared, and fluorescence spectroscopy. The results obtained demonstrate that only one thermodynamically stable gA structure, the antiparallel left-handed double helix β5.6, is formed in this membrane-mimetic environment. The position of the tryptophan fluorescence maximum at 332 nm is the same as that in phospholipid membranes. The causative factors governing the double helix formation in the micellar medium are discussed on the basis of known physicochemical properties of Triton X-100.
- Добавил в систему: Иванов Вадим Тихонович