O-linked glycopeptides retain helicity in water

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

Research output: Contribution to journalArticle

9 Scopus citations

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 - Aug 22 2001

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology

Fingerprint Dive into the research topics of 'O-linked glycopeptides retain helicity in water'. Together they form a unique fingerprint.

  • Cite this