Related Experiment Video
Updated: Jun 6, 2025

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules
Published on: April 25, 2025
Visualizing Dynamic Weak Interaction Networks of Fluorine Atoms within Proteins via NMR
Wenqing Xia1,2, Ling Jiang1,3, Zhou Gong1
1Key Laboratory of Magnetic Resonance in Biological System, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430074, China.
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.
Related Concept Videos
Protein Dynamics in Living Cells
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Other Nuclides: 31P, 19F, 15N NMR
While fluorine-19 and phosphorous-31 have high natural abundances (100%) and positive gyromagnetic ratios, nitrogen-15 has a low natural abundance and a negative gyromagnetic ratio. However, nitrogen-15 is still preferred over nitrogen-14 (which has a...
¹H NMR: Interpreting Distorted and Overlapping Signals
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are...
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
Noncovalent Attractions in Biomolecules
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
¹H NMR: Long-Range Coupling
In alkenes, spin information is communicated via σ–π overlap, as seen in allylic (four-bond) and homoallylic (five-bond) couplings. These coupling interactions are stronger when the σ bond is parallel to the alkene...

