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- Title
How do proteins avoid becoming too stable? Biophysical studies into metastable proteins.
- Authors
Cabrita, Lisa D; Bottomley, Stephen P
- Abstract
The vast majority of theoretical and experimental folding studies have shown that as a protein folds, it attempts to adopt a conformation that occurs at its lowest free energy minimum. However, studies on a small number of proteins have now shown that this is a generality. In this review we discuss recent data on how two proteins, alpha-lytic protease and alpha1-antitrypsin, successfully fold to their metastable native states, whilst avoiding more stable but inactive conformations.
- Publication
European biophysics journal : EBJ, 2004, Vol 33, Issue 2, p83
- ISSN
0175-7571
- Publication type
Journal Article
- DOI
10.1007/s00249-003-0356-1