투고논문

Abstract ¹⁹F nuclear magnetic resonance (NMR) spectroscopy has been acknowledged as a powerful method for investigating the structure, dynamics, and related functional features of challenging protein systems. Because fluorine is absent in native biological systems, ¹⁹F NMR provides highly sensitive, background-free spectra that alleviate the molecular weight limitations and spectral crowding, common yet challenging issues to conventional biomolecular NMR. Following our ¹⁹F NMR review series, in this mini-review, we examine and compare the principles, advantages, limitations, and key applications of widely adopted protein ¹⁹F labeling strategies: biosynthetic incorporation of fluorinated amino acids, cysteine-targeted modification, genetic code expansion, transglutaminase-mediated enzymatic labeling of glutamines, and lysine-targeted modification. This comprehensive comparison establishes a practical guide for selecting optimal ¹⁹F labeling strategies for challenging pharmacological targets and macromolecular complexes.

Keywords NMR spectroscopy, ¹⁹F NMR, protein labeling, protein structure and function

* Address correspondence to: Jin Hae Kim, Department of New Biology, Daegu Gyeongbuk Institute of Science &Technology, Daegu 42988, Republic of Korea, Tel: 82-53-785-1770; E-mail: jinhaekim@dgist.ac.kr