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Small, but Powerful and Attractive: F in Biomolecular NMR

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Journal Structure
Publisher Cell Press
Date 2022 Jan 7
PMID 34995480
Citations 31
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Abstract

Nuclear magnetic resonance (NMR) spectroscopy is a versatile tool for probing structure, dynamics, folding, and interactions at atomic resolution. While naturally occurring magnetically active isotopes, such as H, C, or N, are most commonly used in biomolecular NMR, with N and C isotopic labeling routinely employed at the present time, F is a very attractive and sensitive alternative nucleus, which offers rich information on biomolecules in solution and in the solid state. This perspective summarizes the unique benefits of solution and solid-state F NMR spectroscopy for the study of biological systems. Particular focus is on the most recent studies and on future unique and important potential applications of fluorine NMR methodology.

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References
1.
Zheng W, Zhang Z, Ye Y, Wu Q, Liu M, Li C . Phosphorylation dependent α-synuclein degradation monitored by in-cell NMR. Chem Commun (Camb). 2019; 55(75):11215-11218. DOI: 10.1039/c9cc05662a. View

2.
Ropson I, Frieden C . Dynamic NMR spectral analysis and protein folding: identification of a highly populated folding intermediate of rat intestinal fatty acid-binding protein by 19F NMR. Proc Natl Acad Sci U S A. 1992; 89(15):7222-6. PMC: 49678. DOI: 10.1073/pnas.89.15.7222. View

3.
Klein-Seetharaman J, Getmanova E, Loewen M, Reeves P, Khorana H . NMR spectroscopy in studies of light-induced structural changes in mammalian rhodopsin: applicability of solution (19)F NMR. Proc Natl Acad Sci U S A. 1999; 96(24):13744-9. PMC: 24135. DOI: 10.1073/pnas.96.24.13744. View

4.
Wang M, Lu M, Fritz M, Quinn C, Byeon I, Byeon C . Fast Magic-Angle Spinning F NMR Spectroscopy of HIV-1 Capsid Protein Assemblies. Angew Chem Int Ed Engl. 2018; 57(50):16375-16379. PMC: 6279522. DOI: 10.1002/anie.201809060. View

5.
Campos-Olivas R, Aziz R, Helms G, Evans J, Gronenborn A . Placement of 19F into the center of GB1: effects on structure and stability. FEBS Lett. 2002; 517(1-3):55-60. DOI: 10.1016/s0014-5793(02)02577-2. View