波谱学杂志2017，Vol.34Issue(2)：137-147,11.DOI:10.11938/cjmr20170202
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
摘要
Abstract
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.关键词
液体核磁共振(liquid NMR)/蛋白质/谱峰特性/化学位移归属Key words
liquid NMR/protein/resonance characteristics/chemical shift assignment分类
数理科学引用本文复制引用
李双利,朱勤俊,刘买利,杨运煌..蛋白质分子核磁共振谱峰的特性及其化学位移归属[J].波谱学杂志,2017,34(2):137-147,11.基金项目
国家自然科学基金资助项目(21575155). （21575155）
