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Search for the most stable folds of protein chains: II. Computation of stable architectures of β-proteins using a self-consistent molecular field theoryстатья
Информация о цитировании статьи получена из
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Дата последнего поиска статьи во внешних источниках: 7 июля 2021 г.
- Авторы: Reva Boris A., Finkelstein Alexei V.
- Журнал: Protein Engineering, Design and Selection
- Том: 9
- Номер: 5
- Год издания: 1996
- Издательство: Oxford University Press
- Местоположение издательства: United Kingdom
- Первая страница: 399
- Последняя страница: 411
- DOI: 10.1093/protein/9.5.399
- Аннотация: In a preceding paper we presented a novel approach to computation of 3-D folds of protein chains from their amino acid sequences. This approach is a physically correct generalization of the 'threading' methods. It is based on a self-consistent molecular field theory and on a physical theory of protein folding patterns, which make it possible to examine all the variety of 'potentially stable' folding patterns and all the variety of the chain conformations within each of them and to determine the thermodynamically stable structure. In this paper, we apply this approach to single out stable folding patterns and conformations for the chains of beta-sandwich proteins and show that the similarity of the calculated and observed structures is usually rather close.
- Добавил в систему: Финкельштейн Алексей Витальевич