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Peptoid residues and β‐turn formation
Author(s) -
Rainaldi Mario,
Moretto Vittorio,
Crisma Marco,
Peggion Evaristo,
Mammi Stefano,
Toniolo Claudio,
Cavicchioni Giorgio
Publication year - 2002
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.392
Subject(s) - peptoid , turn (biochemistry) , chemistry , stereochemistry , biochemistry , peptide
A set of terminally protected tripeptoids containing a residue of either N ‐methylglycine or N ‐ iso butylglycine in position i + 1/ i + 2 were synthesized and tested for intramolecularly H‐bonded β‐turn formation. By exploiting FT‐IR absorption and 1 H NMR techniques, their folding tendencies were compared with those of a variety of reference peptides. The amount of β‐turn induction and the relative extent of the various types of intramolecularly H‐bonded β‐turn conformers were determined in chloroform solution. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.