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How the Serpin α(1)-Proteinase Inhibitor Folds

Serpins are remarkable and unique proteins in being able to spontaneously fold into a metastable conformation without the aid of a chaperone or prodomain. This metastable conformation is essential for inhibition of proteinases, so that massive serpin conformational change, driven by the favorable en...

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Библиографические подробности
Главные авторы: Dolmer, Klavs, Gettins, Peter G. W.
Формат: Artigo
Язык:Inglês
Опубликовано: American Society for Biochemistry and Molecular Biology 2012
Предметы:
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC3320992/
https://ncbi.nlm.nih.gov/pubmed/22334651
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M111.315465
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