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Influence of organization of native protein structure on its folding: Modeling of the folding of $\upalpha$-helical proteinsстатья
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 марта 2022 г.
- Авторы: Glyakina A.V., Galzitskaya O.V.
- Журнал: Biochemistry (Moscow)
- Том: 75
- Номер: 8
- Год издания: 2010
- Издательство: Pleiades Publishing, Ltd
- Местоположение издательства: Road Town, United Kingdom
- Первая страница: 995
- Последняя страница: 1005
- DOI: 10.1134/s0006297910080079
- Аннотация: An important question that is addressed here is whether the modeling of protein folding can catch the difference between the folding of proteins with similar structures but with different folding mechanisms. In this work, the modeling of folding of four alpha-helical proteins from the homeodomain family, which are similar in size, was done using the Monte Carlo and dynamic programming methods. A frequently observed order of folding of alpha-helices for each protein was determined using the Monte Carlo method. A correlation between the experimental folding rate and the number of Monte Carlo steps was also demonstrated. Amino acid residues that are important for the folding were determined using the dynamic programming method. The defined regions correlate with the order of folding of secondary-structure elements in the proteins both in experiments and in modeling.
- Добавил в систему: Галзитская Оксана Валериановна