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 glycopeptide 1 was synthesized using a new solid phase synthesis of carbohydrates and a convergent coupling to peptide followed by deprotection. Its conformational properties were subjected to NMR analysis and compared 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 bias suggestive of an equilibrium between an ordered and a random state. The implications of this ordering effect for the larger issue of protein folding are considered.
Laboratory for Nucleic Acid and Protein Structure, Sloan-Kettering Institute for Cancer Research, New York, NY 10021, USA.
D H
DH
Live
R A
RA
Kumar
X
X
Beebe
S J
SJ
Danishefsky
D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D006020:Glycopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D006023:Glycoproteins / Q000737:chemistry*; D006031:Glycosylation; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary
D006020:Glycopeptides; D006023:Glycoproteins