Peptoid residues and β‐turn formation

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Abstract
A set of terminally protected tripeptoids containing a residue of either N‐methylglycine or N‐isobutylglycine in position i + 1/i + 2 were synthesized and tested for intramolecularly H‐bonded β‐turn formation. By exploiting FT‐IR absorption and 1H 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.