Conformational preferences of oligopeptides rich in α-aminoisobutyric acid. III. Design, synthesis and hydrogen bonding in 310-helices
✍ Scribed by BINDRA, VANDANA A. ;KUKI, ATSUO
- Book ID
- 115099707
- Publisher
- Wiley (Blackwell Publishing)
- Year
- 2009
- Tongue
- English
- Weight
- 939 KB
- Volume
- 44
- Category
- Article
- ISSN
- 0367-8377
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📜 SIMILAR VOLUMES
The analysis of the factors that control the helical folding of Aib-rich peptides is extended to include sensitivity to sequence patterns, and in particular the presence of contiguous non-Aib a-mono-alkylated residues. The distinct hydrogen-bonding network of the 310helix, as contrasted with that of
Computer simulations have been used to design a polypeptide with a 3 10 helix conformation. The study has been been performed taking advantage of the intrinsic helix forming tendency of ␣-Aminoisobutyric acid. In order to avoid the formation of the ␣ helix, which is the other common helical conforma