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Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probeстатья
Информация о цитировании статьи получена из
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Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 4 марта 2022 г.
- Авторы: Semisotnov G.V., Rodionova N.A., Razgulyaev O.I., Uversky V.N., Gripas\textquotesingle A.F., Gilmanshin R.I.
- Журнал: Biopolymers
- Том: 31
- Номер: 1
- Год издания: 1991
- Издательство: John Wiley & Sons Inc.
- Местоположение издательства: United States
- Первая страница: 119
- Последняя страница: 128
- DOI: 10.1002/bip.360310111
- Аннотация: Binding of the hydrophobic florescent probe, 1-anilino-naphthalene-8-sulfonate (ANS), to synthetic polypeptides and proteins with a different structural organization has been studied. It has been shown that ANS has a much stronger affinity to the protein "molten globule" state, with a pronounced secondary structure and compactness, but without a tightly packed tertiary structure as compared with its affinity to the native and coil-like proteins, or to coil-like, alpha-helical, or beta-structural hydrophilic homopolypeptides. The possibility of using ANS for the study of equilibrium and kinetic molten globule intermediates is demonstrated, with carbonic anhydrase, beta-lactamase, and alpha-lactalbumin as examples.
- Добавил в систему: Семисотнов Геннадий Васильевич