𝔖 Bobbio Scriptorium
✦   LIBER   ✦

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

No coin nor oath required. For personal study only.


📜 SIMILAR VOLUMES


Conformational preferences of oligopepti
✍ Gautam Basu; Atsuo Kuki 📂 Article 📅 1992 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 977 KB

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

Chain conformation in polyretropeptides
✍ Carlos Alemán 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 139 KB 👁 1 views

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