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

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.
AuthorsC G Long, M H Li, J Baum, B Brodsky
JournalJournal of molecular biology (J Mol Biol) Vol. 225 Issue 1 Pg. 1-4 (May 05 1992) ISSN: 0022-2836 [Print] Netherlands
PMID1583683 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)
Chemical References
  • Peptides
  • Glycine
Topics
  • Circular Dichroism
  • Glycine (chemistry)
  • Kinetics
  • Magnetic Resonance Spectroscopy
  • Peptides (chemistry)
  • Protein Conformation
  • Temperature

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