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-Reference-Cited by-同舟云学术

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

Published:1999-12-15 Issue:3 Volume:266 Page:977-985
ISSN:0014-2956
Container-title:European Journal of Biochemistry
language:en
Short-container-title:European Journal of Biochemistry

Author:

Aumelas André,Chiche Laurent,Kubo Shigeru,Chino Naoyoshi,Watanabe Takushi X.,Kobayashi Yuji

Publisher

Wiley

Subject

Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.1432-1327.1999.00940.x/fullpdf

Reference36 articles.

1. [Lys(-2)-Arg(-1)]endothelin-1 solution structure by two-dimensional 1H-NMR: possible involvement of electrostatic interactions in native disulfide bridge formation and in biological activity decrease.;Aumelas;Biochemistry,1995

2. Improvement of the oxidative folding of endothelin-1 by the Lys-Arg extension at the amino terminus: Implication of a salt-bridge between Arg−1 and Asp8.;Kubo;Lett. Peptide Sci.,1997

3. Formation of native disulfide bonds in endothelin-1. Structural evidence for the involvement of a highly specific salt bridge between the prosequence and the endothelin-1 sequence.;Aumelas;Biochemistry,1998

4. Conformational study of endothelins and sarafotoxins with the cystine-stabilized helical motif by means of CD spectra.;Tamaoki;Biopolymers,1992

5. Folding motifs induced and stabilized by distinct cystine frameworks.;Tamaoki;Protein Eng.,1998

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