Structure of peptides and polypeptides in the solid state as elucidated by NMR chemical shift
Structure of peptides and polypeptides in the solid state as elucidated by NMR chemical shift
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DOI：
10.1016/s0022-2860(97)00299-8
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发表时间：
1998-01-30
影响因子：
3.8
通讯作者：
Kurosu, H
中科院分区：
文献类型：
--
作者：
Ando, I;Kameda, T;Kurosu, H
通过对固态C-13核磁共振化学位移的观察，已经成功地阐明了多肽、多肽和蛋白质在固态状态下的主链构象和氢键结构，将固态C-13核磁共振与量子化学化学位移计算相结合是结构表征的有力手段。此外，还简要介绍了N-15和O-17原子核的固体核磁共振对获得氢键结构的信息是非常有用的。本文综述了近年来我们利用高分辨率固体核磁共振光谱及其与量子化学计算相结合对固态多肽和多肽（包括蛋白质）的结构表征所做的工作。(C) 1998爱思唯尔科学有限公司
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.