In common with the homologous 3,3-difluoro- and 3,3,3-trifluoro-species, 3-fluoro-1,2-epoxypropane is a small chiral molecule with a simple rotational spectrum, making it potentially useful for chiral analysis via conversion of enantiomers into spectroscopically distinct diastereomers through formation of noncovalently bound complexes. The rotational spectrum of 3-fluoro-1,2-epoxypropane (FO) and of its heterodimer with the argon atom are obtained, along with several isotopologues of each, using Fourier transform microwave spectroscopy from 5.6 to 18.1 GHz, and their structures determined. Surprisingly, the structure of 3-fluoro-1,2-epoxypropane-argon does not show a strong similarity to those previously determined for 3,3-difluoro-1,2-epoxypropane-argon and 3,3,3-trifluoro-1,2-epoxypropane-argon but instead is more analogous to that of propylene oxide-argon. Equilibrium structural parameters and mapped electrostatic potential surfaces obtained via quantum chemistry calculations are used in rationalizing this result.We utilize various computational methodologies to study menthol's interaction with multiple organic phases, a lipid bilayer, and the human α4β2 nicotinic acetylcholine receptor (nAChR), the most abundant nAChR in the brain. First, force field parameters developed for menthol are validated in alchemical free energy perturbation simulations to calculate solvation free energies of menthol in water, dodecane, and octanol and compare the results against experimental data. Next, umbrella sampling is used to construct the free energy profile of menthol permeation across a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) bilayer. The results from a flooding simulation designed to study the water-membrane partitioning of menthol in a POPC lipid bilayer are used to determine the penetration depth and the preferred orientation of menthol in the bilayer. Finally, employing both docking and flooding simulations, menthol is shown to bind to different sites on the human α4β2 nAChR. The most likely binding mode of menthol to a desensitized membrane-embedded α4β2 nAChR is identified to be via a membrane-mediated pathway in which menthol binds to the sites at the lipid-protein interface after partitioning in the membrane. A rare but distinct binding mode in which menthol binds to the extracellular opening of receptor's ion permeation pore is also reported.A quinoline-based hexadentate ligand, (S,S)-N,N,N',N'-tetrakis(6-methoxy-2-quinolylmethyl)-1,2-diphenylethylenediamine ((S,S)-6-MeOTQPh2EN), exhibits fluorescence enhancement at 498 nm upon addition of 1 equiv of Zn2+ (IZn/I0 = 12, φZn = 0.047) in aqueous DMF solution (DMF/H2O = 21). Addition of 1 equiv of Cd2+ affords a much smaller fluorescence increase at the same wavelength (ICd/I0 = 2.5, ICd/IZn = 21%). The trivalent metal ions such as Al3+, Cr3+, and Fe3+ also exhibit fluorescence enhancement at 395 nm (IAl/I0 = 22, ICr/I0 = 6 and IFe3+/I0 = 13). In contrast, meso-6-MeOTQPh2EN exhibits a Cd2+-selective fluorescence increase at 405 nm in the presence of 1 equiv of metal ion (ICd/I0 = 11.5, φCd = 0.022), while Zn2+ induces a smaller fluorescent response under the same experimental conditions (IZn/I0 = 3.3, IZn/ICd = 29%). In this case, the fluorescence intensities of meso-6-MeOTQPh2EN in the presence of a large amount of Zn2+ and Cd2+ become similar. This diastereomer-dependent, fluorescent metal ion specificity is derived from the Zn2+-specific intramolecular excimer formation in (S,S)-6-MeOTQPh2EN-Zn2+ complex and higher binding affinity of meso-6-MeOTQPh2EN with Cd2+ in comparison to Zn2+.  https://www.selleckchem.com/products/bms-927711.html  The more conformationally restricted diastereomeric pair, namely, cis- and trans-TQDACHs (cis- and trans-N,N,N',N'-tetrakis(2-quinolylmethyl)-1,2-diaminocyclohexanes), both exhibit Zn2+-specific fluorescence enhancement because of the high metal binding affinity and intramolecular excimer forming property derived from the rigid DACH backbone.Nitrogen is ubiquitous in both natural and laboratory-grown diamond, but the number and nature of the nitrogen-containing defects can have a profound effect on the diamond material and its properties. An ever-growing fraction of the supply of diamond appearing on the world market is now lab-grown. Here, we survey recent progress in two complementary diamond synthesis methods-high pressure high temperature (HPHT) growth and chemical vapor deposition (CVD), how each is allowing ever more precise control of nitrogen incorporation in the resulting diamond, and how the diamond produced by either method can be further processed (e.g., by implantation or annealing) to achieve a particular outcome or property. The burgeoning availability of diamond samples grown under well-defined conditions has also enabled huge advances in the characterization and understanding of nitrogen-containing defects in diamond-alone and in association with vacancies, hydrogen, and transition metal atoms. Among these, the negatively charged nitrogen-vacancy (NV-) defect in diamond is attracting particular current interest in account of the many new and exciting opportunities it offers for, for example, quantum technologies, nanoscale magnetometry, and biosensing.Penicillin binding proteins (PBPs) catalyzing transpeptidation reactions that stabilize the peptidoglycan component of the bacterial cell wall are the targets of β-lactams, the most clinically successful antibiotics to date. However, PBP-transpeptidation enzymology has evaded detailed analysis, because of the historical unavailability of kinetically competent assays with physiologically relevant substrates and the previously unappreciated contribution of protein cofactors to PBP activity. By re-engineering peptidoglycan synthesis, we have constructed a continuous spectrophotometric assay for transpeptidation of native or near native peptidoglycan precursors and fragments by Escherichia coli PBP1B, allowing us to (a) identify recognition elements of transpeptidase substrates, (b) reveal a novel mechanism of stereochemical editing within peptidoglycan transpeptidation, (c) assess the impact of peptidoglycan substrates on β-lactam targeting of transpeptidation, and (d) demonstrate that both substrates have to be bound before transpeptidation occurs.