Crystal structures of collagen model peptides with Pro-Hyp-Gly repeating sequence at 1.26 Å resolution: Implications for proline ring puckering

Biopolymers - Peptide Science Section

Volumn 76, Issue 5, 2004, Pages 367-377

  Okuyama, Kenji ^a   Hongo, Chizuru ^a   Fukushima, Rie ^a   Wu, Guanghan ^a   Narita, Hirotaka ^a   Noguchi, Keiichi ^a   Tanaka, Yuji ^b   Nishino, Norikazu ^b  

^a TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

^b KYUSHU INSTITUTE OF TECHNOLOGY   (Japan)

Author keywords

Collagen; Crystal structure; Hydroxyproline; Triple helix

Indexed keywords

AMINO ACIDS; CONFORMATIONS; CRYSTAL SYMMETRY; HYDRATION; HYDROXYLATION; SYNCHROTRON RADIATION; THERMAL EFFECTS;

PROLINE; ROOM TEMPERATURE (RT);

COLLAGEN;

COLLAGEN; HYDROXYPROLINE; PEPTIDE; PROLINE;

ARTICLE; CRYSTAL STRUCTURE; HYDRATION; HYDROXYLATION; MOLECULAR MODEL; NUCLEOTIDE REPEAT; PROTEIN CONFORMATION; ROOM TEMPERATURE; SEQUENCE ANALYSIS; SYNCHROTRON RADIATION; TRIPLE HELIX;

COLLAGEN; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; HYDROXYPROLINE; OLIGOPEPTIDES; PROLINE; PROTEIN CONFORMATION; TEMPERATURE; WATER;

EID: 9144246166     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/bip.20107     Document Type: Article

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