Sequential individual resonance assignments in the 1H‐NMR spectra of polypeptides and proteins
Sequential individual resonance assignments in the 1H‐NMR spectra of polypeptides and proteins
复制标题
多肽和蛋白质 1H-NMR 谱中的连续个体共振分配
作者：
K. Wüthrich
最近，引入了一种新的蛋白质1H-nmr光谱归属方法，该方法依赖于多肽中质子-质子距离的立体化学考虑，以及使用二维nmr获得1H-1H通过键和通过空间连接图。在本文中，更详细地讨论了这种分配过程的一个特定方面，即，如何从氨基酸侧链自旋系统的识别和氨基酸序列中相邻残基的识别中获得单个共振分配。
Recently, a new procedure for the assignment of protein 1H‐nmr spectra was introduced that relies on stereochemical considerations of proton–proton distances in polypeptides and on the use of two‐dimensional nmr for obtaining 1H‐1H through‐bond and through‐space connectivity maps. In the present paper a particular aspect of this assignment procedure is discussed in more detail, i.e., how to obtain individual resonance assignments from identification of amino acid side‐chain spin systems and identification of neighboring residues in the amino acid sequence.
核磁共振的距离几何分析
DOI：
10.1111/j.1399-3011.1981.tb01978.x
发表时间：
1981
期刊：
International journal of peptide and protein research
影响因子：
--
作者：
Crippen,GM;Oppenheimer,NJ;Connolly,ML
通讯作者：
Connolly,ML