Folding of peptide models of collagen and misfolding in disease

Jean Baum, Barbara Brodsky

Research output: Contribution to journalArticlepeer-review

112 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)122-128
Number of pages7
JournalCurrent Opinion in Structural Biology
Issue number1
StatePublished - Feb 1 1999

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

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