蛋白质分子核磁共振谱峰的特性及其化学位移归属

Characteristics of Protein NMR Resonances and Chemical Shift Assignments

尽可能完全、准确地归属蛋白质分子的核磁共振(Nuclear Magnetic Resonance,NMR)谱峰,是解析可信赖、高质量的蛋白质三维空间溶液结构的首要条件.自动归属软件的开发和应用,已经方便并加快了蛋白质分子核磁共振谱峰的归属进程.然而,对蛋白质核磁共振研究领域的新手来说,因为缺乏对蛋白质分子的核磁共振谱峰特性的系统认识而可能发生对自动归属结果的错误指认或指认不完全,从而导致蛋白质结构解析的错误或偏差.该文针对蛋白质分子中的核磁共振谱峰特性,比如同位素效应和立体异构等,结合具体的蛋白质分子的核磁共振实验图谱,进行了较为详尽的论述,期望对从事蛋白质核磁共振的研究者在理解蛋白质分子的核磁共振谱峰特性及其归属方面有所裨益.

Complete and correct chemical shift assignments of NMR resonances are critical to obtain a reliable and high-quality three-dimensional protein structure with liquid NMR spectroscopy.For experts in the field,the use of auto-assignment software programs can facilitate and expedite the process of protein resonance assignments.However,correct understanding and application of the auto-assignment results can be challenging for those who are new to the field and without sufficient knowledge of NMR resonance characteristics of the atoms in a protein.Incomplete or wrong chemical shift assignments will lead to deviations or even mistakes in the calculation of protein structure.In attempt to provide a better understanding of protein NMR resonances and chemical shift assignments for those are new to this field,we reviewed protein NMR resonance characteristics,such as isotope effect and conformational stereoisomer,in this paper.Examples were given to facilitate understanding.