Structure of peptides and polypeptides in the solid state as elucidated by NMR chemical shift

被引:39
作者
Ando, I [1 ]
Kameda, T [1 ]
Asakawa, N [1 ]
Kuroki, S [1 ]
Kurosu, H [1 ]
机构
[1] Tokyo Inst Technol, Dept Polymer Chem, Meguro Ku, Tokyo, Japan
关键词
solid-state NMR spectroscopy; conformation; hydrogen bonding; peptides; polypeptides;
D O I
10.1016/S0022-2860(97)00299-8
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
It is reviewed that through the observation of solid-state C-13 NMR chemical shift, the main-chain conformation and hydrogen-bonded structure of peptides, polypeptides and proteins in the solid state have been successfully elucidated, and the combination of solid stale C-13 NMR and chemical shift calculation by quantum chemistry is a powerful means for the structural characterization. Furthermore, it is briefly introduced that solid state NMR of N-15 and O-17 nuclei is very useful for obtaining information about hydrogen-bonded structure. This review article is communicated on the basis of our recent works on structural characterization of peptides and polypeptides including proteins in the solid state by high-resolution solid-state NMR spectroscopy and its combination with quantum chemical calculation. (C) 1998 Elsevier Science B.V.
引用
收藏
页码:213 / 230
页数:18
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