Using 19F magic angle spinning (MAS) nuclear magnetic resonance (NMR) spectroscopy, we show that most of the fluoride present in the KGa-lb reference kaolinite from Washington County, Georgia, occurs as a surface-adsorbed species bonded to Al. This surface fluoride can be removed from the <2 µm fraction by acid wash, but is largely retained in the coarse fraction. Correlation of integrated 19F NMR peak intensities with fluoride sorption experiments indicates a bulk F content of ∼144 ppm for KGa-1b, of which ∼30% substitutes for hydroxyl sites in the mineral structure and the remaining 70% occurs adsorbed on particle surfaces, corresponding to an edge surface fluoride density of ∼0.7 F− nm−2. 19F{27Al} TRAPDOR (TRAnsfer of Populations in DOuble Resonance) NMR data for the original kaolinite and for products of F− sorption experiments at pH 4 show that all of the observed 19F signals arise from fluoride bonded to Al atoms. Furthermore, bridging Al-F-Al sites and terminal Al-F give distinctly different TRAPDOR fractions allowing assignment of resolved peaks based on the number of Al in the first coordination sphere. This result was confirmed for fluoride adsorbed to the surface of gibbsite from aqueous suspension. No evidence was found for Si-F-type environments on the kaolinite surfaces.

The binding capacity of the L-leucine receptor from Escherichia coli was measured with L-phenylalanine and 4-fluoro-L-phenylalanine as substrates by fluorescence. The apparent dissociation constants (KD) for L-leucine, L-phenylalanine, and 4-fluoro-L-phenylalanine are 0.40, 0.18, and 0.26 respectively. 19F NMR data show protein-induced shifts for the 4-fluoro-L-phenylalanine peak and 3-fluoro-L-phenylalanine when receptor is present. Evidence points to the binding of only the L-isomers of these fluorine analogs.