๐”– Bobbio Scriptorium
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Analysis of disulfide bonds in protein structures

โœ 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

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Search for allosteric disulfide bonds in
โœ Bryan Schmidt; Philip J Hogg ๐Ÿ“‚ Article ๐Ÿ“… 2007 ๐Ÿ› BioMed Central ๐ŸŒ English โš– 747 KB

## 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 in prote
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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