Design of Secondary Structures in Unnatural Peptides: Stable Helical γ-Tetra-, Hexa-, and Octapeptides and Consequences of α-Substitution
Author:
Affiliation:
1. Department of Chemistry, Université de Montréal, C.P. 6128 Succursale Centre-ville, Montréal, Québec H3C 3J7 Canada
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja9814671
Reference20 articles.
1. The structure of proteins: Two hydrogen-bonded helical configurations of the polypeptide chain
2. Local Interactions in Protein Folding: Lessons from the α-Helix
3. De Novo Design of Native Proteins: Characterization of Proteins Intended To Fold into Antiparallel, Rop-like, Four-Helix Bundles
4. β-Peptides: a surprise at every turn
5. ?-Peptides Forming More Stable Secondary Structures than ?-Peptides: Synthesis and helical NMR-solution structure of the ?-hexapeptide analog of H-(Val-Ala-Leu)2-OH
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