Determination of accurate 19F chemical shift tensors with R-symmetry recoupling at high MAS frequencies (60–100 kHz)

Cell-free synthesis of amyloid fibrils with infectious properties and amenable to sub-milligram magic-angle spinning NMR analysis

“…As observed for the CF-6F-HETs sample, the experimental 19 F line width and the number of observed resonances suggest that the sample is highly homogeneous. Overall, the 1D spectral quality in the 19 F dimension of our CF synthesized samples is excellent and in the range of reported MAS NMR data obtained on small compounds 102 – 105 , amino acids 106 , peptides 107 , 108 and protein samples 100 , 109 – 112 from the Polenova, Gronenborn and Hong laboratories at various magnetic fields and MAS frequencies. Next, to investigate the local effect of fluorine incorporation into the 13 C signals, we conducted a 2D hCH experiment on CF-2F-C-HETs.…”

Chemical Shift Anisotropy: A Promising Parameter To Distinguish the 29Si NMR Peaks in Zeolites

“…This approach was successfully demonstrated in the literature, including 1 H NMR and 19 F NMR studies . Despite its low sensitivity toward asymmetry parameters, this method was selected here to estimate the strength of the CSA coupling only, knowing the potential overlapping of 4 Q 4 (1Al) 29 Si sites for every Al position in the framework in addition to the low amount of Al in the sample (Si/Al = 40).…”

“…32 This approach was successfully demonstrated in the literature, 33 including 1 H NMR 32 and 19 F NMR studies. 34 Despite its low sensitivity toward asymmetry parameters, this method was selected here to estimate the strength of the CSA coupling only, knowing the potential overlapping of 4 Q 4 (1Al) 29 Si sites for every Al position in the framework in addition to the low amount of Al in the sample (Si/Al = 40). The R18 2 5 sequence consists of a continuous series of 180°pulses that alternate in phase by ±50°synchronized such that 18 pulses (9 pairs) are applied during two sample rotational periods about the magic angle.…”

19F Fast Magic-Angle Spinning NMR Spectroscopy on Microcrystalline Complexes of Fluorinated Ligands and the Carbohydrate Recognition Domain of Galectin-3

“…Whereas X-ray crystallography has provided structures for the galectin-3C complexes with the fluorinated ligands, NMR spectroscopy yields complementary insights about local electronic environment and dynamics of ligands as well as the protein using chemical shift and dipolar coupling tensors as exquisitely sensitive reporters. While the current study was performed at the MAS frequencies of up to 60 kHz, we anticipate that faster spinning, with frequencies of 100 kHz and higher, will be advantageous and enable correlation experiments inaccessible with lower frequencies, as demonstrated by us recently. − Together, our results highlight the power of 19 F fast-MAS NMR spectroscopy for investigating protein-fluorinated ligand interactions and provide a toolkit for a broad range of systems, beyond the specific example used here. Finally, we envision that similar approaches will find broad applications for improving existing ligands by guided drug design in a variety of biotechnology and pharmaceutical applications.…”