Comparison of Design Strategies for Promotion of β-Peptide 14-Helix Stability in Water
✍ Scribed by Esther Vaz; William C. Pomerantz; Matthias Geyer; Samuel H. Gellman; Luc Brunsveld
- Book ID
- 102788786
- Publisher
- John Wiley and Sons
- Year
- 2008
- Tongue
- English
- Weight
- 577 KB
- Volume
- 9
- Category
- Article
- ISSN
- 1439-4227
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract Designed octapeptides Boc‐Leu‐Val‐Val‐Aib‐^D^Xxx‐Leu‐Val‐Val‐OMe (^D^Xxx = ^D^Ala, 3a;^D^Val, 3c and ^D^Pro, 5a) and Boc‐Leu‐Phe‐Val‐Aib‐^D^Ala‐Leu‐Phe‐Val‐OMe (3b) have been investigated to construct models of a stable type I′ β‐turn nucleated hairpin and to generate systems for invest
A peptide fragment corresponding to the third helix of Staphylococcus Aureus protein A, domain B, was chosen to study the effect of the main-chain direction upon secondary structure formation and stability, applying the retro-enantio concept. For this purpose, two peptides consisting of the native (