Abstract
The utilization of fluorine probes in protein research has advanced our understanding of the nature of macromolecules. The diverse activities of proteins are governed by intricate weak interaction networks, yet the experimental detection presents a challenge. Herein, we have developed an NMR analytical method based on quantum coherent operations to characterize the weak chemical bonds of fluorine atoms within proteins that are bound to metal fluorides or labeled with fluorinated amino acids. Our approach offers a fast-screening method for identifying a weak interaction network without requiring crystallization.
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