Synthesis, characterization, and conformational analysis by FT-IR absorption, H-1 NMR and X-ray diffraction techniques are described for a series of side-chain O-glycosylated Thr peptides of different main-chain length rich in the helicogenic Aib residue. The results obtained, compared with those of related peptides containing side-chain protected Thr and Ser residues and host Aib homo-oligomers, also reported in this work, provided new information on the preferred conformation of the naturally occurring antifreeze glycopeptides.
Influence of glycosylation on the conformational preferences of folded oligopeptides
M Crisma;
2001
Abstract
Synthesis, characterization, and conformational analysis by FT-IR absorption, H-1 NMR and X-ray diffraction techniques are described for a series of side-chain O-glycosylated Thr peptides of different main-chain length rich in the helicogenic Aib residue. The results obtained, compared with those of related peptides containing side-chain protected Thr and Ser residues and host Aib homo-oligomers, also reported in this work, provided new information on the preferred conformation of the naturally occurring antifreeze glycopeptides.File in questo prodotto:
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