Folding of Disulfide Proteins
Disulfide-containing proteins belong to a unique class of proteins for studying the mechanism of protein folding. Their folding mechanism can be analyzed by three distinct techniques: (1) The conventional denaturation-renaturation method (disulfide intact); (2) The disulfide oxidation method (oxidat...
| Other Authors: | , |
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| Format: | eBook |
| Language: | English |
| Published: |
New York, NY
Springer New York
2011, 2011
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| Edition: | 1st ed. 2011 |
| Series: | Protein Reviews
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| Subjects: | |
| Online Access: | |
| Collection: | Springer eBooks 2005- - Collection details see MPG.ReNa |
Table of Contents:
- Oxidative folding: coupling conformational folding and disulfide formation
- The case of oxidative folding of ribonuclease A: Factors impacting fold maturation of ER-processed proteins
- Cystine knot folding in cyclotides
- In vitro folding of single chain/double chain insulin and related protein
- Unfolding and refolding of disulfide proteins via disulfide scrambling
- Small catalysts for Protein oxidative folding
- Protein Disulfide Isomerase and the Catalysis of Oxidative Protein Folding
- Allosteric disulfide bonds
- The problem of expression of multi-disulfide bonded recombinant protein in E. coli
- NMR-spectroscopic investigation of disulfide dynamics in unfolded states of proteins
- A half-century of oxidative folding and protein disulfide formation