High-resolution X-ray structure of the unexpectedly stable dimer of the [Lys(-2)-Arg(-1)-des(17-21)]endothelin-1 peptide

Biochemistry

Volumn 43, Issue 48, 2004, Pages 15154-15168

  Hoh, François ^a   Cerdan, Rachel ^a   Kaas, Quentin ^a   Nishi, Yoshinori ^c   Chiche, Laurent ^a   Kubo, Shigeru ^b   Chino, Naoyoshi ^b   Kobayashi, Yuji ^c   Dumas, Christian ^a   Aumelas, André ^a,d  

^a CENTRE DE BIOCHIMIE STRUCTURALE   (France)

^b Peptide Institute Inc   (Japan)

^c OSAKA UNIVERSITY   (Japan)

^d UNIV MONTPELLIER   (France)

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTALS; HYDROPHOBICITY; MOLECULAR DYNAMICS; STRUCTURAL ANALYSIS;

INTRAMOLECULAR; PEPTIDES;

DIMERS;

DISULFIDE; ENDOTHELIN 1 DERIVATIVE;

AB INITIO CALCULATION; ACIDITY; AQUEOUS SOLUTION; ARTICLE; BETA SHEET; CRYSTALLIZATION; DIMERIZATION; DISULFIDE BOND; HYDROPHOBICITY; HYPOTHESIS; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; SEDIMENTATION; SIMULATION; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; DIPEPTIDES; DISULFIDES; ENDOTHELIN-1; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN FOLDING; PROTEIN PRECURSORS; SALTS; SOLUTIONS; TEMPERATURE; THERMODYNAMICS;

EID: 10044256408     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049098a     Document Type: Article

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