CONFORMATIONAL INFLUENCES OF GLYCOSYLATION OF A PEPTIDE - A POSSIBLE MODEL FOR THE EFFECT OF GLYCOSYLATION ON THE RATE OF PROTEIN-FOLDING

Improved strategies for synthesis make it possible to expand the range of glycopeptides available for detailed conformational studies. The g lycopeptide I was synthesized using a new solid phase synthesis of car bohydrates and a convergent coupling to peptide followed by deprotecti on. Its conformational properties were subjected to NMR analysis and c ompared with a control peptide 2 prepared by conventional solid phase methods. Whereas peptide 2 fails to manifest any appreciable secondary structure, the glycopeptide 1 does show considerable conformational b ias suggestive of an equilibrium between an ordered and a random state . The implications of this ordering effect for the larger issue of pro tein folding are considered.