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- W1907134976 abstract "Understanding the folding pathway of α1-antitrypsin is of interest from both biomedical and fundamental molecular biology perspectives. The native fold of α1-antitrypsin is metastable, and therefore does not represent the most stable conformation that its primary sequence can adopt. More stable conformations are formed when the reactive center loop inserts, as the fourth strand, into the A β sheet. The accessibility of these alternative low-energy folds renders α1-antitrypsin susceptible to mutations that can result in dysfunction and pathology. Here, I review some of the literature from the past 20 years, which has examined how α1-antitrypsin folds and preserves its native metastable state. In addition, I look at the relationship between α1-antitrypsin folding and misfolding, and its role in disease." @default.
- W1907134976 created "2016-06-24" @default.
- W1907134976 creator A5088390473 @default.
- W1907134976 date "2012-12-20" @default.
- W1907134976 modified "2023-09-24" @default.
- W1907134976 title "The Folding Pathway of α1-Antitrypsin" @default.
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