Secondary structure of ShK toxin, a potassium-channel-blocking peptide

被引：6

作者：

Kem, WR

Sanyal, G

Williams, RW

Pennington, MW

机构：

[1] UNIV FLORIDA,COLL MED,DEPT PHARM & THERAPEUT,GAINESVILLE,FL 32610

[2] MERCK SHARP & DOHME RES LABS,DEPT VACCINE PHARMACEUT RES,W POINT,PA 19486

[3] UNIFORMED SERV UNIV HLTH SCI,DEPT BIOCHEM,BETHESDA,MD 20814

[4] BACHEM BIOSCI INC,KING OF PRUSSIA,PA 19406

来源：

LETTERS IN PEPTIDE SCIENCE | 1996年 / 3卷 / 02期

关键词：

peptide; secondary structure; Raman; CD; potassium-channel toxin; sea anemone;

D O I：

10.1007/BF00126735

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Sea anemones possess small K-channel-blocking peptides about the same size as the scorpion K-channel toxins. We have estimated the secondary structure content (33% helix, 26% beta-sheet) of one of these toxins, ShK toxin, using CD, Raman, and FTIR spectroscopy. A hypothetical 3D structure of the peptide core has been constructed using secondary structure and disulfide-linkage constraints; a single helical segment running from Ala(14) through Leu(25) is predicted.

引用

页码：69 / 72

页数：4

共 20 条

[1] A POTASSIUM CHANNEL TOXIN FROM THE SECRETION OF THE SEA-ANEMONE BUNODOSOMA-GRANULIFERA - ISOLATION, AMINO-ACID-SEQUENCE AND BIOLOGICAL-ACTIVITY [J].