Application of Nuclear Magnetic Resonance Spectroscopy for Studying Protein Three-dimensional Structure
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School of Chemistry, Key Laboratory for Polymeric Composite and Functional Materials of Ministry of Education, Guangdong Provincial Key Laboratory for High Performance Polymer-based Composites, Sun Yat-sen University, Guangzhou 510275, China

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This work was supported by a grant from the Key Project of Guangdong Natural Science Foundation of China(2017B030311007)

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    Abstract:

    The unique three-dimensional structure of protein is closely related to its biological function. Therefore, investigating the three-dimensional structure of protein is helpful to reveal its biological function mechanism. The study of protein three-dimensional structure in the solution state using nuclear magnetic resonance (NMR) spectroscopy can accurately reveal the relationship between protein structure and biological function. The aim of this article is to provide an effective strategy for accurate analysis of protein three-dimensional structure using NMR and combination with other biophysical means such as molecular modeling and computation methods through reviewing the research progress and latest technology in these fields. Firstly, we summarize the theory of NMR for studying protein three-dimensional structure. Secondly, we deeply review the theory and technology of NMR analysis of protein three-dimensional structure, including isotope labeling of proteins (labeling methods, expression systems, and purification techniques), NMR data acquisition and analysis software, analysis of amino acid sequence, secondary structural unit and three-dimensional structure of protein using NMR and combination with other biophysical means (F?rster/fluorescence resonance energy transfer (FRET), chemical cross-linking coupled with mass spectrometry (CXMS), small angel X-ray scattering (SAXS), and cryo-electron microscopy (Cryo-EM)), and analysis of excited state structure of protein molecules using Carr-Purcell-Meiboom-Gill relaxation dispersion (CPMG RD) and chemical exchange saturation transfer (CEST) techniques. Thirdly, we overview recent researches about application of NMR for analysis of three-dimensional structure of high molecular mass single chain protein and supramolecular protein complex. Fourthly, we elaborate the latest progress in the field of NMR combined with molecular modeling and computation methods. Lastly, we summarize challenges and prospects of application of NMR for studying protein three-dimensional structure in the future.

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YIN Lin, SHEN Jun-Cheng, YANG Li-Qun. Application of Nuclear Magnetic Resonance Spectroscopy for Studying Protein Three-dimensional Structure[J]. Progress in Biochemistry and Biophysics,2022,49(7):1273-1290

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History
  • Received:March 16,2021
  • Revised:October 12,2021
  • Accepted:October 18,2021
  • Online: July 20,2022
  • Published: July 20,2022