Disulphide bonds and protein folding
โ Scribed by Geisow, M. J.
- Book ID
- 109706932
- Publisher
- Nature Publishing Group
- Year
- 1977
- Tongue
- English
- Weight
- 345 KB
- Volume
- 269
- Category
- Article
- ISSN
- 0028-0836
- DOI
- 10.1038/269009a0
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The best-characterized model pathway of protein folding, that of disulphide bond formation in the small protein BPTI, has been questioned recently. A reinvestigation of that pathway, using alternative methods, concluded that the intermediates with non-native disulphide bonds accumulated to lower lev
The properties of disulphide bonds relevant to their roles in stabilizing protein conformation are reviewed. Natural disulphides can stabilize folded conformations substantially, in some cases to much greater extents than would be expected from just entropic eflects on the unfolded state. The linkag