A H-1-NMR DETERMINATION OF THE SOLUTION STRUCTURE OF THE A-CHAIN OF INSULIN - COMPARISON WITH THE CRYSTAL-STRUCTURE AND AN EXAMINATION OF THE ROLE OF SOLVENT

被引：8
作者：
HAWKINS, BL
CROSS, KJ
CRAIK, DJ
机构：
[1] MONASH UNIV,VICTORIAN COLL PHARM,PARKVILLE,VIC 3052,AUSTRALIA
[2] PETER MACCALLUM CANC INST,NMR FACIL,PARKVILLE,VIC 3052,AUSTRALIA
来源：
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1994年 / 1209卷 / 02期
关键词：
INSULIN A-CHAIN; NMR; H-1-; SOLUTION STRUCTURE; (BOVINE);
D O I：
10.1016/0167-4838(94)90182-1
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 H-1-NMR chemical shift assignments for the oxidized A-chain of bovine insulin have been determined in aqueous and 30% trinuoroethanol/water solutions. Analysis of the observed medium-range nuclear Overhauser effects indicates that in aqueous solution significant populations of the peptide exist, with a 3(10)-helical conformation over residues 12-17. This region corresponds to helix A (13-20) in the crystal structure of the 2 Zn insulin hexamer. In 30% TFE solution, the NOE data are supportive of a random coil conformation throughout the peptide.
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页码：177 / 182
页数：6
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