O-linked glycopeptides retain helicity in water

M. M. Palian, N. E. Jacobsen, Robin L Polt

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

A 17-residue O-linked glycopeptide model incorporating a central α-mannosyl serine residue, and its unglycosylated analog both demonstrate substantial helicity in water. The peptide sequence was derived from previous studies in which differences in overall helicity as a function of single amino acid substitutions were measured by circular dichroism (CD). The helical content was predicted by molecular modeling, and confirmed by CD and NMR. Moreover, the glycopeptide retained its helicity in the presence of SDS micelles, whereas the native peptide lost secondary structure in the presence of micelles. The inference is that the peptide sequence is a more important helix determinant than glycosylation per se.

Original languageEnglish (US)
Pages (from-to)180-189
Number of pages10
JournalJournal of Peptide Research
Volume58
Issue number2
DOIs
StatePublished - 2001

Fingerprint

Glycopeptides
Dichroism
Micelles
Circular Dichroism
Peptides
Water
Glycosylation
Molecular modeling
Amino Acid Substitution
Serine
Substitution reactions
Nuclear magnetic resonance
Amino Acids

Keywords

  • α-helix
  • Circular dichroism
  • Conformational analysis
  • Glycopeptide
  • Glycoside
  • NMR
  • O-linked
  • SDS micelles
  • Secondary structure

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology

Cite this

O-linked glycopeptides retain helicity in water. / Palian, M. M.; Jacobsen, N. E.; Polt, Robin L.

In: Journal of Peptide Research, Vol. 58, No. 2, 2001, p. 180-189.

Research output: Contribution to journalArticle

Palian, M. M. ; Jacobsen, N. E. ; Polt, Robin L. / O-linked glycopeptides retain helicity in water. In: Journal of Peptide Research. 2001 ; Vol. 58, No. 2. pp. 180-189.
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