Chinese Journal of Magnetic Resonance ›› 2021, Vol. 38 ›› Issue (4): 523-532.doi: 10.11938/cjmr20212931

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NMR Studies of Large Protein Dynamics Using Unnatural Amino Acids

Chao-wei SHI,Pan SHI,Chang-lin TIAN*()   

  1. Hefei National Laboratory of Physical Science at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei 230027, China
  • Received:2021-07-02 Online:2021-12-05 Published:2021-08-26
  • Contact: Chang-lin TIAN E-mail:cltian@ustc.edu.cn

Abstract:

Nuclear magnetic resonance (NMR) is a major method used to study protein structure at atomic resolution. Besides presenting the high-resolution structure, NMR facilitates studies on protein dynamics near physiological conditions that are intimately related to the biological mechanism of the proteins. Unnatural amino acids (UAA) labeling could significantly reduce the complexity of protein NMR spectra. In this review, we briefly summarize the widely used UAA labeling strategies for proteins, including chemical peptide synthesis, residue-specific peptide modification, 19F labeled aromatic amino acids incorporation and genetic code expansion based UAA incorporation. The recent applicants of UAA in characterizing protein structure and dynamics, the limitations and prospects of UAA are also highlighted.

Key words: solution NMR, solid-state NMR, unnatural amino acid, large size protein

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