NMR evidence for Mg(II) binding to N1 of ATP.

The conformation of the complex of [ATP-Mg]2+ is studied by 1H, 15N and 31P NMR on ATP in the absence and presence of MgCl2 in a wide pH range from 1 to 10. 1H-15N HMBC experiments show a large change in the 15N chemical shift of N1 up to 10 ppm around pH 3.7, suggesting that there is a strong interaction between Mg2+ and N1 of ATP at this pH. 31P NMR indicates that at pH 3.7 the phosphate chain also binds Mg2+. 1H diffusion measurements imply that the [ATP-Mg]2+ complex involves only one ligand and one metal ion.

Diffusion-broadened velocity spectra of convection in variable-temperature BP-LED experiments.

When NMR diffusion experiments are performed at temperatures different from ambient temperature, temperature gradients due to probe design can cause thermal convection and therefore significantly affect the signal amplitude. Fourier transformation of the signal amplitude gives rise to a diffusion-broadened velocity spectrum, which contains information about the convection velocity. It is shown that when the diffusion broadening factor is smaller than the maximum velocity, the broadening has little effect on the determination of the maximum velocity. Thus, convection velocity can be determined in the presence of diffusion.

Binding site of Zn2+ in ATP:N1 at low pH and N7 at high pH as evidenced by 1H-15N NMR HMBC experiments.

Nuclear magnetic resonance (NMR) 1H-15N heteronuclear multiple bond correlation (HMBC) experiments on natural abundant adenosine-5'-triphosphate (ATP) showed that zinc(II) induced large chemical shifts (> 10 ppm) for N1 at lower pH (2-5) while for N7 at higher pH (5-7), suggesting that the binding site of Zn2+ in the purine base of ATP is pH dependent. The size effect of zinc(II) in coordination is also discussed.

NMR observation of hydrolysis of acetonitrile to acetamide catalyzed by binuclear silver cryptate.

NMR analyses (TOCSY, HMQC and DOSY) indicate that, in the presence of water, acetonitrile is exclusively hydrolyzed to acetamide catalyzed by bisilver cryptate complex, which contains coordinating acetonitrile molecule.

NMR diffusion and relaxation study of drug-protein interaction.

In this work, NMR diffusion and relaxation measurements are applied to the study of the interaction between the anti-inflammatory drug salicylate and the human serum albumin (HSA) in solutions. The self-diffusion coefficients and the spin-lattice relaxation rates of salicylate are measured as a function of the concentration. The dissociation constant, Kd, for drug/HSA complexes and the number of binding sites, n, are evaluated.

CP/MAS 13C spectral editing of dried pine leaves.

The recently developed CP/MAS 13C spectral editing technique is applied to the study of the structure of the dried Australian pine leaves. Subspectra of quaternary carbon C, methenyl CH, methylene CH2 and methyl CH3 for Australian pine leaves have been obtained. Simple formulae for spectral editing are proposed.

The first solid-state 171Yb nuclear magnetic resonance spectra.

The first powder and magic-angle spinning (MAS) experiments on 171Yb are reported. The divalent ytterbium compound RbYbI3 was studied by solid-state 171Yb nuclear magnetic resonance (NMR) and a powder spectrum of axial symmetry was obtained. The principal components of the chemical shielding tensor were determined as sigma 11 = sigma 22 = -62 ppm and sigma 33 = 124 ppm. An inversion-recovery experiment showed an anisotropic relaxation behavior with the parallel component relaxing faster than the perpendicular component (T1 perpendicular = 426 ms, T1 parallel = 298 ma). The natural line width of 800 Hz, which corresponds to an effective T2 of 0.4 ms, was obtained from the MAS spectrum.