The conformational effects of N-glycosylation on the tailpiece from serum IgM.

@article{Wormald1991TheCE,
  title={The conformational effects of N-glycosylation on the tailpiece from serum IgM.},
  author={Mark R Wormald and E. W. Wooten and Renzo Bazzo and Christopher J. Edge and Arnold Feinstein and Thomas W. Rademacher and Raymond A. Dwek},
  journal={European journal of biochemistry},
  year={1991},
  volume={198 1},
  pages={131-9}
}
1H-NMR spectroscopy has been used to study the conformation and dynamics of the isolated tailpiece from human serum immunoglobulin M, a 22-residue peptide containing a single asparagine glycosylation site. The peptide is isolated as a set of glycoforms, varying only in the sequence of the oligosaccharide attached at the glycosylation site. The oligosaccharides present have the general formula (Man)n(GlcNAc)2, with 45% having n = 6, 45% having n = 8 and 10% having n = 7 and/or 9. They have been… CONTINUE READING

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