THE CHEMICAL-SHIFT INDEX - A FAST AND SIMPLE METHOD FOR THE ASSIGNMENT OF PROTEIN SECONDARY STRUCTURE THROUGH NMR-SPECTROSCOPY
THE CHEMICAL-SHIFT INDEX - A FAST AND SIMPLE METHOD FOR THE ASSIGNMENT OF PROTEIN SECONDARY STRUCTURE THROUGH NMR-SPECTROSCOPY
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DOI：
10.1021/bi00121a010
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发表时间：
1992-02-18
期刊：
影响因子：
2.9
通讯作者：
RICHARDS, FM
中科院分区：
文献类型：
--
作者：
WISHART, DS;SYKES, BD;RICHARDS, FM
Wishart et al. (1991) [j] .中华医学杂志。（出版中）]已经证明了H-1核磁共振化学位移强烈依赖于蛋白质二级结构的特征和性质。特别是，已经发现所有20种天然存在的氨基酸的α - ch质子的H-1 NMR化学位移在螺旋结构中经历了向上场位移（相对于随机线圈值），而在β链扩展结构中经历了类似的向下场位移。在这些观察的基础上，描述了一种基于α - ch -1共振分配的简单检查，快速定量地确定蛋白质中二级结构元件的身份，范围和位置的技术。提供了一些例子来证明该技术的简单性和准确性。这种新方法被发现几乎与更传统的基于noe的确定二级结构的方法一样准确，并且可以证明在最近的顺序分配技术发展中特别有用，这些技术现在几乎与noe无关[Ikura， M., Kay， L. E., & Bax， A.（1990）生物化学29,4659-4667]。我们建议，这种新的程序不应该被视为替代现有的二级结构确定的严格方法，而是应该被视为这些方法的补充。
Previous studies by Wishart et al. [Wishart, D. S., Sykes, B. D., & Richards, F. M. (1991) J. Mol. Biol. (in press)] have demonstrated that H-1 NMR chemical shifts are strongly dependent on the character and nature of protein secondary structure. In particular, it has been found that the H-1 NMR chemical shift of the alpha-CH proton of all 20 naturally occurring amino acids experiences an upfield shift (with respect to the random coil value) when in a helical configuration and a comparable downfield shift when in a beta-strand extended configuration. On the basis of these observations, a technique is described for rapidly and quantitatively determining the identity, extent, and location of secondary structural elements in proteins based on the simple inspection of the alpha-CH H-1 resonance assignments. A number of examples are provided to demonstrate both the simplicity and the accuracy of the technique. This new method is found to be almost as accurate as the more traditional NOE-based methods of determining secondary structure and could prove to be particularly useful in light of the recent development of sequential assignment techniques which are now almost NOE-independent [Ikura, M., Kay, L. E., & Bax, A. (1990) Biochemistry 29, 4659-4667]. We suggest that this new procedure should not necessarily be seen as a substitute to existing rigorous methods for secondary structure determination but, rather, should be viewed as a complement to these approaches.