NMR shows hydrophobic interactions replace glycine packing in the triple helix at a natural break in the (Gly-X-Y)n repeat

Journal of Biological Chemistry

Volumn 282, Issue 31, 2007, Pages 22699-22706

  Li, Yingjie ^a   Brodsky, Barbara ^b   Baum, Jean ^a  

^a RUTGERS UNIVERSITY   (United States)

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

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; HYDROPHOBICITY; MOLECULAR INTERACTIONS; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

COLLAGEN MODEL PEPTIDES; NATURAL BREAK; STRUCTURAL CONSEQUENCES; TRIPLE-HELICAL STRUCTURES;

AMINO ACIDS;

COLLAGEN TYPE 4; GLYCINE;

AMINO ACID SEQUENCE; ARTICLE; HYDROPHOBICITY; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; TRIPLE HELIX;

AMINO ACID SEQUENCE; COLLAGEN TYPE IV; GLYCINE; HYDROGEN BONDING; HYDROPHOBICITY; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; THERMODYNAMICS;

EID: 34547949571     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M702910200     Document Type: Article

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