Nuclear magnetic resonance and circular dichroism studies of a triple-helical peptide with a glycine substitution

Cynthia Gwynne Long, Ming Hua Li, Jean Baum, Barbara Brodsky

Research output: Contribution to journalArticlepeer-review

32 Scopus citations

Abstract

The triple-helical conformation has the stringent amino acid sequence constraint that every third residue must be a glycine, (X-Y-Gly)n. We use nuclear magnetic resonance and circular dichroism to quantify the consequences of a substitution in the glycine position of a triple-helical peptide, and to enhance our understanding of interactions in this basic structural motif. A 30-residue peptide with a Gly → Ala change forms a stable trimer at a folding rate somewhat less than that of the unsubstituted peptide, and the substitution results in a marked decrease in thermal stability and a conformational perturbation of about 30% of the triple-helical structure. Two models were generated for this peptide, one with the alanine residues packed inside the triple helix and one with a looping out of the chain at the substitution site. Studies on the Gly → Ala peptide are useful in understanding connective tissue diseases which result from the substitution of one glycine residue in the triple-helix of fibrillar collagens.

Original languageEnglish (US)
Pages (from-to)1-4
Number of pages4
JournalJournal of molecular biology
Volume225
Issue number1
DOIs
StatePublished - May 5 1992

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

Keywords

  • circular dichroism spectroscopy
  • collagen
  • n.m.r.
  • peptide
  • triple-helix

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