Premium
Conformational study of endothelins and sarafotoxins with the cystine‐stabilized helical motif by means of CD spectra
Author(s) -
Tamaoki Haruhiko,
Kyogoku Yoshimasa,
Nakajima Kiichiro,
Sakakibara Shumpei,
Hayashi Mitsuo,
Kobayashi Yuji
Publication year - 1992
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360320410
Subject(s) - chemistry , endothelins , stereochemistry , cystine , crystallography , endothelin receptor , biochemistry , cysteine , receptor , enzyme
A series of CD measurements were carried out on members of peptides in the endothelin and sarafotoxin families. The helical structures taken by these peptides containing the helical motif with the sequences of Cys‐X‐X‐X‐Cys and Cys‐X‐Cys [Y. Kobayashi et al. (1991) Neurochemistry International Vol. 18, pp. 525–534] are classified into three groups: a group of structures of ET‐1, ET‐2 and vasoactive intestinal contractor (VIC), a group of sarafotoxin, and a group of ET‐3.