Folding of peptide models of collagen and misfolding in disease

Curr Opin Struct Biol. 1999 Feb;9(1):122-8. doi: 10.1016/s0959-440x(99)80016-5.

Abstract

The misfolding of the triple helix has been shown to play a critical role in collagen diseases. Normal and mutated collagen triple helices can be modeled by short, synthetic peptides of varying design. NMR spectroscopy and circular dichroism studies on the assembly of these peptide models have recently been used to isolate specific steps in the folding pathway and have provided information on the alterations resulting from mutations.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Circular Dichroism
  • Collagen / chemistry*
  • Collagen / genetics
  • Collagen Diseases / genetics
  • Collagen Diseases / metabolism*
  • Humans
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation
  • Osteogenesis Imperfecta / genetics
  • Osteogenesis Imperfecta / metabolism
  • Peptides / chemistry
  • Protein Folding

Substances

  • Peptides
  • Collagen