In achiral PFAS with 2–3 CF₂ groups, long-lived ¹⁹F spin states (T_LLS) were measured and found to last about 3× longer than T₁ in a static 11.6 T field. These lifetimes are sensitive to macromolecular binding, making them useful for screening fluorinated drugs. T_LLS and T₁ are expected to increase at lower fields where ¹⁹F CSA effects are weaker.

Proteins structure and motion are key to their function. Using electron paramagnetic resonance (EPR) methods, it is possible to measure distances between magnetic markers like gadolinium ions grafted on proteins. Such measurements rely on the gadolinium phase memory time, determining how long the signal lasts. We studied how nearby atoms and environmental noise affect signal lifetime using advanced EPR techniques. Our findings show how lifetime can be extended to design better protein analysis.

A protein was produced, where a single amino acid type was substituted globally by a fluorinated analogue, delivering multiple sites for interrogation by ¹⁹F-NMR spectroscopy. Substitution of methyl groups by CH₂F groups yields outstanding spectral resolution with minimal structural perturbation of the protein. Our work identifies the γ-gauche effect as the main reason for the spectral dispersion.

3D printed sample cells, inserted into standard 5-mm NMR tubes, are demonstrated to offer improved sensitivity for biomolecular NMR when the quantity of material is limiting. By using an ellipsoidal shape, magnetic field homogeneity inside the microcell to first order is insensitive to differences in the magnetic susceptibility of printer resin and solvent. The sample cells are particularly useful at high ionic strength and at ultra-high magnetic fields.