HYDROGEN-BOND LENGTH AND N-15 NMR CHEMICAL-SHIFT OF THE GLYCINE RESIDUE OF SOME OLIGOPEPTIDES IN THE SOLID-STATE

被引：38

作者：

KUROKI, S ^{[1
]}

ASAKAWA, N ^{[1
]}

ANDO, S ^{[1
]}

ANDO, I ^{[1
]}

SHOJI, A ^{[1
]}

OZAKI, T ^{[1
]}

机构：

[1] GUNMA UNIV,DEPT BIOL SCI,KIRYU,GUNMA 376,JAPAN

来源：

JOURNAL OF MOLECULAR STRUCTURE | 1991年 / 245卷 / 1-2期

关键词：

D O I：

10.1016/0022-2860(91)87007-5

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

CP-MAS and CP-static N-15 NMR spectra were measured for a variety of solid oligopeptides containing the glycine residue, the crystal structures of which had already been determined by X-ray diffraction. From the results of the observed N-15 chemical shifts, it was found that the isotropic N-15 chemical shifts (sigma-iso) of the glycine residues move downfield with a decrease of hydrogen bond length (R(N)...o) between the nitrogen and oxygen atoms in the amide groups, and the principal value of sigma-33 moves linearly downfield with a decrease of R(N)...o. There is no relationship between the principal value of sigma-11 or sigma-22 and R(N)...o. This indicates that such a linear downfield shift of sigma-33 contributes predominantly to the downfield shift of sigma-iso. Quantum chemical calculations of the N-15 shielding constant for the model compounds were carried out by the FPT-INDO method, and the relationship between N-15 chemical shift and R(N)...o discussed.

引用

页码：69 / 80

页数：12

共 24 条

[1] CONFORMATION-DEPENDENT C-13 NMR CHEMICAL-SHIFTS OF POLY(L-ALANINE) IN THE SOLID-STATE - FPT INDO CALCULATION OF N-ACETYL-N'-METHYL-L-ALANINE AMIDE AS A MODEL-COMPOUND OF POLY(L-ALANINE) [J].