A H-1-NMR STUDY OF THE SOLUTION CONFORMATION OF THE NEUROPEPTIDE GALANIN

被引：37

作者：

WENNERBERG, ABA

COOKE, RM

CARLQUIST, M

RIGLER, R

CAMPBELL, ID

机构：

[1] KAROLINSKA INST,DEPT MED BIOPHYS,S-10401 STOCKHOLM 60,SWEDEN

[2] UNIV OXFORD,DEPT BIOCHEM,OXFORD OX1 3QU,ENGLAND

[3] KAROLINSKA INST,DEPT BIOCHEM 2,S-10401 STOCKHOLM 60,SWEDEN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 166卷 / 03期

关键词：

D O I：

10.1016/0006-291X(90)90980-2

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：

The conformations of the neuropeptide galanin in water and trifluoroethanol solutions have been examined by 1H NMR spectroscopy. Analysis of two-dimensional NMR experiments enabled the assignment of virtually all the 1H resonances of galanin in trifluoroethanol solution and many of the 1H resonances in aqueous solution. Interpretation of the NMR data in structural terms suggests that in trifluoroethanol galanin is predominantly helical while in water it does not adopt a fixed conformation. © 1990.

引用

页码：1102 / 1109

页数：8

共 34 条

[1] MECHANISM OF GALANIN-INHIBITED INSULIN RELEASE - OCCURRENCE OF A PERTUSSIS-TOXIN-SENSITIVE INHIBITION OF ADENYLATE-CYCLASE [J].