Transformation of the mechanism of triple-helix peptide folding in the absence of a C-terminal nucleation domain and its implications for mutations in collagen disorders

Journal of Biological Chemistry

Volumn 279, Issue 45, 2004, Pages 46890-46895

  Buevich, Alexei V ^a,c   Silva, Teresita ^b   Brodsky, Barbara ^b   Baum, Jean ^a  

^a RUTGERS UNIVERSITY   (United States)

^b RUTGERS ROBERT WOOD JOHNSON MEDICAL SCHOOL   (United States)

^c MERCK RESEARCH LABORATORIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; DISEASES; MICROSCOPIC EXAMINATION; MUTAGENS; NUCLEAR MAGNETIC RESONANCE; NUCLEATION; SUBSTITUTION REACTIONS;

COLLAGEN DISEASES; MUTATIONS; OSTEOGENESIS;

POLYPEPTIDES;

GLYCINE; MUTANT PROTEIN; PEPTIDE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; COLLAGEN DISEASE; GENE MUTATION; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE; OSTEOGENESIS IMPERFECTA; PRIORITY JOURNAL; PROTEIN DEFECT; PROTEIN FOLDING; TRIPLE HELIX;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; COLLAGEN; COLLAGEN DISEASES; GLYCINE; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDES; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SERINE; TEMPERATURE; TIME FACTORS;

EID: 8744229956     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M407061200     Document Type: Article

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