HYDROGEN-BONDING STRUCTURAL STUDY OF SOLID PEPTIDES AND POLYPEPTIDES CONTAINING A GLYCINE RESIDUE BY O-17 NMR-SPECTROSCOPY

被引:53
作者
KUROKI, S
TAKAHASHI, A
ANDO, I
SHOJI, A
OZAKI, T
机构
[1] TOKYO INST TECHNOL,DEPT POLYMER CHEM,MEGURO KU,TOKYO 152,JAPAN
[2] GUNMA UNIV,DEPT BIOL SCI,KIRYU,GUNMA 376,JAPAN
关键词
D O I
10.1016/0022-2860(94)07993-5
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
Static O-17 NMR spectra of polyglycines I and II and glycylglycine peptides in the solid state were measured by the cross polarization technique. By computer simulations of these spectra, three NMR parameters (quadrupolar coupling constant (e2qQ/h), electric field gradient asymmetry parameter (eta(Q)), and chemical shift (delta)) were determined. From these results, it was found that as the hydrogen bond length decreased, the e2qQ/h value decreased. Furthermore, the principal values of the O-17 chemical shift tensor for both the peptides and polypeptides moved upfield with a decrease in the hydrogen bond length. From these experimental findings, it was clarified that O-17 NMR spectroscopy can provide a useful means of elucidating the hydrogen-bonding structure in solid peptides and polypeptides.
引用
收藏
页码:197 / 208
页数:12
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