4.8 Article

Generating Five Independent Molecular Alignments for Simultaneous Protein Structure and Dynamics Determination Using Nuclear Magnetic Resonance Spectroscopy

期刊

ANALYTICAL CHEMISTRY
卷 92, 期 23, 页码 15263-15269

出版社

AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.0c02882

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资金

  1. National Natural Science Foundation of China [31600690, 31872725, 21773280]
  2. Shandong Provincial Natural Science Foundation [ZR2018ZB0207]
  3. Taishan Scholars Program of Shandong Province [ts201712077]
  4. DICPQIBEBT [DICPQIBEBT UN201802]
  5. Dalian National Laboratory For Clean Energy (DNL) of CAS [QIBEBT I201928]

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Residual dipolar couplings (RDCs) are commonly used in NMR for protein structure and dynamics studies, but it is challenging to generate five independent RDC data sets (required for simultaneous structure and dynamics determination) for most protein molecules in the magnetic field. In this work, a reporter protein with a lanthanide tag is introduced to create five independent alignments. This reporter protein is then attached to target proteins where five independent sets of RDCs are also obtained for the target proteins. The fitting of RDCs provides important information about the structure and dynamics of the target proteins. The method is simple and effective and, in principle, can be used to generate complete sets of RDCs for different protein molecules.

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