Conformational preferences of oligopeptides rich in α-aminoisobutyric acid. III. Design, synthesis and hydrogen bonding in 310-helices
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3011.1994.tb01142.x/fullpdf
Reference26 articles.
1. Conformational preferences of oligopeptides rich in α-aminoisobutyric acid. I. Observation of a 310/α-helical transition upon sequence permutation
2. Structural characteristics of .alpha.-helical peptide molecules containing Aib residues
3. Non coded Cα,α-disubstituted amino acids
4. Tetrahedron;Bosch;Helv. Chim. Acta,1982
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