This book aims to cover the knowledge of protein folding accumulated from studies of disulfide-containing proteins, including methodologies, folding pathways, and folding mechanism of numerous extensively characterized disulfide proteins. Folding of Disulfide Proteins will be valuable supplementary
Thioredoxin-Catalyzed Refolding of Disulfide-Containing Proteins
β Scribed by Vincent P. Pigiet and Barbara J. Schuster
- Book ID
- 123633239
- Publisher
- National Academy of Sciences
- Year
- 1986
- Tongue
- English
- Weight
- 899 KB
- Volume
- 83
- Category
- Article
- ISSN
- 0027-8424
- DOI
- 10.2307/28150
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## Abstract Based on the structural characteristic of Protein disulfide isomerases and DsbA that have hydrophobic regions around the active sites, hydrophobic alkyl tails are linked to cystamine to create new small molecular foldase mimics, acyl cystamine. Both the oxidizing power and oxidation spe
## Background Expression systems based on self-cleavable intein domains allow the generation of recombinant proteins with a C-terminal thioester. This uniquely reactive C-terminus can be used in native chemical ligation reactions to introduce synthetic groups or to immobilize proteins on surfaces a