CONFORMATIONAL-ANALYSIS OF 4 BETA-METHYLPHENYLALANINE STEREOISOMERS IN A BIOACTIVE PEPTIDE BY Z-FILTERED RELAY NMR-SPECTROSCOPY

被引：19

作者：

KOVER, KE ^{[1
]}

JIAO, D ^{[1
]}

FANG, S ^{[1
]}

HRUBY, VJ ^{[1
]}

机构：

[1] UNIV ARIZONA,DEPT CHEM,TUCSON,AZ 85721

来源：

MAGNETIC RESONANCE IN CHEMISTRY | 1993年 / 31卷 / 12期

关键词：

H-1; NMR; C-13; CONFORMATIONAL ANALYSIS; SIDE-CHAIN CONFORMATION; Z-FILTERED RELAY SPECTROSCOPY; HOMONUCLEAR AND HETERONUCLEAR VICINAL COUPLING CONSTANTS;

D O I：

10.1002/mrc.1260311208

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The rotamer populations around the C-alpha-C-beta bond of amino acid residues with one beta-proton can be calculated from homonuclear and heteronuclear vicinal coupling constants. The measurement of long-range heteronuclear coupling constants, however, suffers from the inherent low sensitivity of the heteronuclear multiple bond experiments. In this paper it is demonstrated that z-filtered homonuclear and heteronuclear relay spectroscopy provides a sensitive and accurate means for the evaluation of conformationally important vicinal coupling constants. Side-chain conformations of the four stereoisomers of beta-methylphenylalanine residues in synthetic octapeptide analogues of CCK-8 were derived from the measured coupling constants. This information is not easily available from conformational analysis based on simple steric considerations.

引用

页码：1072 / 1076

页数：5

共 29 条

[1] MLEV-17-BASED TWO-DIMENSIONAL HOMONUCLEAR MAGNETIZATION TRANSFER SPECTROSCOPY [J].