A research team led by Shi Chaowei from the University of Science and Technology of China (USTC) of the Chinese Academy of Sciences (CAS) has adapted the fluoride ion channel protein Fluc-Ec1 combined with deuterium substitution and 19F labeling methods, paving a new path for membrane protein nuclear magnetic resonance (NMR) research.
but also observes their dynamic characteristics. These insights are invaluable for understanding the functional mechanisms of large biomolecules such as proteins. With the advancement of high-speed magic-angle spinning technology, the resolution of solid-state NMR spectroscopy was significantly improved. Theoretically, it surpasses the molecular weight limitations of liquid NMR, gradually being applied to the study of dynamic conformations of complex biomolecular systems.
However, the challenges of low signal strength and resolution remain, limiting its widespread application in solid-state biomolecular NMR research. Hydrogen and , due to their high gyromagnetic ratios and strong NMR signals, emerge as ideal candidates for NMR observation., has a unique structure and demonstrates high selectivity towards fluoride ions. The researchers investigated the Fluc-Ec1 conformation in phospholipid bilayers and introduced 4--l-phenylalanine into the vestibule space by the codon extension method.
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