Polarity of disulfide bonds
β Scribed by Aleister J. Saunders; Gregory B. Young; Gary J. Pielak
- Publisher
- Cold Spring Harbor Laboratory Press
- Year
- 1993
- Tongue
- English
- Weight
- 158 KB
- Volume
- 2
- Category
- Article
- ISSN
- 0961-8368
No coin nor oath required. For personal study only.
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Proteolytic digests of human antithrombin 111 (ATIII) have heen analyzed by a combination of reversed-phase high-performance liquid chromatography and fast atom bombardment (FAB) mass spectrometry for disulfidecontaining peptides which are diagnostic for disulfide linkages in ATIII. These results in
## 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