We synthesized and tested for intramolecularly H-bonded beta-turn formation a set of terminally protected tripeptoids containing in position i+1/i+2 either a residue of N-methylglycine or of N-isobutylglycine. By exploiting FT-IR absorption and 1H NMR techniques we compared their folding tendencies 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 beta-Turn Formation
RAINALDI, MARIO;PEGGION, EVARISTO;MAMMI, STEFANO;TONIOLO, CLAUDIO;
2002
Abstract
We synthesized and tested for intramolecularly H-bonded beta-turn formation a set of terminally protected tripeptoids containing in position i+1/i+2 either a residue of N-methylglycine or of N-isobutylglycine. By exploiting FT-IR absorption and 1H NMR techniques we compared their folding tendencies 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.
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