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Theoretical Study of a Landscape of Protein Folding−Unfolding Pathways. Folding Rates at Midtransitionстатья
Статья опубликована в высокорейтинговом журнале
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: 15 июля 2021 г.
- Авторы: Ivankov Dmitry N., Finkelstein Alexei V.
- Журнал: Biochemistry
- Том: 40
- Номер: 33
- Год издания: 2001
- Издательство: American Chemical Society
- Местоположение издательства: United States
- Первая страница: 9957
- Последняя страница: 9961
- DOI: 10.1021/bi010625p
- Аннотация: This paper presents a new method for calculating the folding-unfolding rates of globular proteins. The method is based on solution of kinetic equations for a network of folding-unfolding pathways of the proteins. The rates are calculated in the point of thermodynamic equilibrium between the native and completely unfolded states. The method has been applied to all the proteins listed by Jackson [Jackson, S. E. (1998) Folding Des. 3, R81-R91] and some peptides. Although the studied protein chains differ by more than 1 order of magnitude in size and exhibit two- as well as three-state kinetics in water, and their folding rates cover more than 11 orders of magnitude, the theoretical estimates are reasonable close to the experimentally measured folding rates in midtransition (the correlation coefficient being as high as 0.78). This means that the presented theory (having no adjustable parameters at all) is consistent with the experimental observations.
- Добавил в систему: Финкельштейн Алексей Витальевич