A set of terminally protected tripeptoids containing a residue of either N-methylglycine or N-isobutylglycine in position i+l/i+2 were synthesized and tested for intramolecularly H-bonded beta-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 beta-turn induction and the relative extent of the various types of intramolecularly H-bonded beta-turn conformers were determined in chloroform solution.

Peptoid residues and β-turn formation

CAVICCHIONI, Giorgio
2002

Abstract

A set of terminally protected tripeptoids containing a residue of either N-methylglycine or N-isobutylglycine in position i+l/i+2 were synthesized and tested for intramolecularly H-bonded beta-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 beta-turn induction and the relative extent of the various types of intramolecularly H-bonded beta-turn conformers were determined in chloroform solution.
2002
Rainaldi, M.; Moretto, V.; Crisma, M.; Peggion, E.; Mammi, S.; Toniolo, C.; Cavicchioni, Giorgio
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11392/1200621
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