Crystal structure of (Gly-Pro-Hyp)9: Implications for the collagen molecular model

Biopolymers

Volumn 97, Issue 8, 2012, Pages 607-616

  Okuyama, Kenji ^a   Miyama, Keita ^a   Mizuno, Kazunori ^b   Bächinger, Hans Peter ^b,c  

^a OSAKA UNIVERSITY   (Japan)

^b SHRINERS HOSPITAL FOR CHILDREN   (United States)

^c OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

collagen; collagen helix; collagen model peptide; crystal structure; Gly Pro Hyp; triple helix

Indexed keywords

ALTERNATIVE STRUCTURE; AMINO ACID SEQUENCE; COLLAGEN-MODEL PEPTIDE; GLY-PRO-HYP; HELICAL CONFORMATION; HELICAL SYMMETRY; IN-FIBER; MOLECULAR MODELS; REPEATING UNIT; TRIPLE HELIXES; TYPICAL SEQUENCES; X RAY FIBER DIFFRACTION;

AMINO ACIDS; CRYSTAL STRUCTURE; DIFFRACTION; MOLECULAR STRUCTURE; PEPTIDES;

COLLAGEN;

COLLAGEN; GLYCINE; HYDROXYPROLINE; PROLINE;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DATA ANALYSIS; HUMAN; MOLECULAR MODEL; PEPTIDE ANALYSIS; PROTEIN CONFORMATION; PROTEIN STRUCTURE; X RAY DIFFRACTION;

COLLAGEN; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; MODELS, MOLECULAR; OLIGOPEPTIDES; PROLINE; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP; WATER;

EID: 84861319116     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.22048     Document Type: Article

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