Folding of peptide models of collagen and misfolding in disease.
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.
Department of Chemistry, Rutgers University, Piscataway, NJ 08855-0939, USA. Baum@rutchem.rutgers.edu
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D000595:Amino Acid Sequence; D000818:Animals; D002942:Circular Dichroism; D003094:Collagen / Q000737:chemistry* / Q000235:genetics; D003095:Collagen Diseases / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D010013:Osteogenesis Imperfecta / Q000235:genetics / Q000378:metabolism; D010455:Peptides / Q000737:chemistry; D017510:Protein Folding
D010455:Peptides; D003094:Collagen