The chimeric peptide [Lys(-2)-Arg(-1)]-sarafotoxin-S6b, composed of the endothelin pro-sequence and sarafotoxin, retains the salt-bridge staple between Arg(-1) and Asp8 previously observed in [Lys(-2)-Arg(-1)]-endothelin. Implications of this salt-bridge in the contractile activity and the oxidative folding reaction

European Journal of Biochemistry

Volumn 266, Issue 3, 1999, Pages 977-985

  Aumelas, André ^a   Chiche, Laurent ^a   Kubo, Shigeru ^b   Chino, Naoyoshi ^b   Watanabe, Takushi X ^b   Kobayashi, Yuji ^c  

^a CNRS   (France)

^b Peptide Institute Inc   (Japan)

^c NONE

Author keywords

Disulfide bond; Endothelin; NMR; Salt bridge; Sarafotoxin

Indexed keywords

ENDOTHELIN 1; SARAFOTOXIN; SARAFOTOXIN S6B;

ARTICLE; CHIMERA; CIRCULAR DICHROISM; DISULFIDE BOND; HYDROGEN BOND; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OXIDATION REDUCTION REACTION; PEPTIDE ANALYSIS; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; DISULFIDES; ENDOTHELIN-1; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PROTEIN STRUCTURE, SECONDARY; RATS; RECOMBINANT FUSION PROTEINS; SALTS; STRUCTURE-ACTIVITY RELATIONSHIP; VASOCONSTRICTOR AGENTS; VIPER VENOMS;

EID: 0033572914     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00940.x     Document Type: Article

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