Chinese Journal of Magnetic Resonance (Dec 2021)

NMR Studies of Large Protein Dynamics Using Unnatural Amino Acids

  • Chao-wei SHI,
  • Pan SHI,
  • Chang-lin TIAN

DOI
https://doi.org/10.11938/cjmr20212931
Journal volume & issue
Vol. 38, no. 4
pp. 523 – 532

Abstract

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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.

Keywords