Covalent Labeling of Human Neuroglobin with a 19F-Probe to Study its Conformational Changes Using 19F NMR
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Updated: Nov 4, 2026

In vivo 19F MRI for Cell Tracking
Published on: November 25, 2013
Si-Qi Xia1, Xi-Chun Liu1, Shu-Qin Gao2
1School of Chemistry and Chemical Engineering, University of South China, Hengyang421001, China.
Abstract:
It is of interest to develop new approaches to probing protein conformational changes and protein-protein interactions. In this study, we covalently labeled human neuroglobin (Ngb) with a 19F-probe containing a Ph-OCF3 group at Cys120 and by introducing cysteine residues at specific positions in the C120S Ngb mutant. 19F NMR provides valuable insights into its conformational changes upon cleavage of the intramolecular disulfide bond of Cys46-Cys55, as well as its interactions with protein partners such as cytochrome c (Cyt c) through the formation of the Ngb-Cyt c complex. This study presents a convenient approach to investigating the dynamic properties of heme globins regulated by disulfide bonds and protein-protein interactions.
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