Conformational preferences of oligopeptides rich in α-aminoisobutyric acid. I. Observation of a 310/α-helical transition upon sequence permutation

Conformational preferences of oligopepti

Conformational preferences of oligopeptides rich in α-aminoisobutyric acid. II. A model for the 310/α-helix transition with composition and sequence sensitivity

✍ 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