The electrochemical reduction of disulfide bonds in proteins. II
β Scribed by Sianette Kwee
- Publisher
- Elsevier Science
- Year
- 1976
- Tongue
- English
- Weight
- 583 KB
- Volume
- 3
- Category
- Article
- ISSN
- 1567-5394
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π SIMILAR VOLUMES
## Abstract An understanding of the forces that contribute to stability is pivotal in solving the proteinβfolding problem. Classical theory suggests that disulfide bonds stabilize proteins by reducing the entropy of the denatured state. More recent theories have attempted to expand this idea, sugge
The thermostable sweet protein brazzein consists of 54 amino acid residues and has four intrumolecular disulfide bonds, the location qf which is unknown. We found that bruzzein resists enzymatic hydrol-vsis at enzyme/substrute ratios ( w / w ) of 1:100-1:10 at 35-40Β°C for 24-48 h. Brazzein wus hjdro