Analysis of disulfide bonds in protein structures
โ Scribed by J. W. H. WONG; P. J. HOGG
- Book ID
- 109154351
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 48 KB
- Volume
- 8
- Category
- Article
- ISSN
- 1538-7933
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
## Background Allosteric disulfide bonds regulate protein function when they break and/or form. They typically have a -RHStaple configuration, which is defined by the sign of the five chi angles that make up the disulfide bond. ## Results All disulfides in NMR and X-ray protein structures as well
Native disulfide bond formation is critical for the proper folding of many proteins. Recent studies using newly identified protein oxidants, folding catalysts, and mutant cells provide insight into the mechanism of oxidative protein folding in vivo. This insight promises new strategies for more effi