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Structures of peptides from α‐amino acids methylated at the α‐carbon ,
Author(s) -
Toniolo C.,
Crisma M.,
Formaggio F.,
Valle C.,
Cavicchioni G.,
Precigoux G.,
Aubry A.,
Kamphuis J.
Publication year - 1993
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360330708
Subject(s) - chemistry , chirality (physics) , amino acid , peptide , depsipeptide , stereochemistry , helix (gastropod) , carbon fibers , biochemistry , ecology , physics , chiral symmetry breaking , materials science , quantum mechanics , snail , composite number , nambu–jona lasinio model , composite material , biology , quark
Abstract The structural preferences of peptides (and depsipeptides) from the achiral MeAib and Hib residues, and the chiral Iva, (αMe) Val, (αMe) Leu, and (αMe) Phe residues, as determined by conformational energy computations, x‐ray diffraction analyses, and 1 H‐nmr and spectroscopic studies, are reviewed and compared with literature data on Aib‐containing peptides. The results obtained indicate that helical structures are preferentially adopted by peptides rich in these α‐amino acids methylated at the α‐carbon. Intriguing experimental findings on the impact of the chirality of Iva, (αMe) Val, and (αMe) Phe residues on helix screw sense are illustrated. © 1993 John Wiley & Sons, Inc.