Characteristics of Protein NMR Resonances and Chemical Shift Assignments

doi:10.11938/cjmr20170202

Abstract

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.

Key words: protein, resonance characteristics, chemical shift assignment, liquid NMR

CLC Number:

O482.53

LI Shuang-li, ZHU Qing-jun, LIU Mai-li, YANG Yun-huang. Characteristics of Protein NMR Resonances and Chemical Shift Assignments[J]. Chinese Journal of Magnetic Resonance, 2017, 34(2): 137-147.

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