Conformational preferences of oligopeptides rich in α‐aminoisobutyric acid. I. Observation of a 310/α‐helical transition upon sequence permutation
- 1 December 1991
- journal article
- research article
- Published by Wiley in Biopolymers
- Vol. 31 (14) , 1763-1774
- https://doi.org/10.1002/bip.360311410
Abstract
The solution conformation of peptides rich in the α,α‐dialkylated amino acid Aib has proven to be a subtle problem, not because of helix/coil transitions, but rather because of α‐helical/310‐helical competition. A special series of peptides containing 75% Aib has been synthesized that feature identical amino acid composition but differing sequences; they are sequence permutation isomers. Nuclear magnetic resonance hydrogen‐bonding studies reveal that there is a sequence permutation induced transition between the two alternative helical forms within this set. The implications for the design and conformational prediction of helical Aib‐rich peptides are discussed.Keywords
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