J Phys Chem B Vol. 113 Issue 1

Li-Ion Diffusion in the Equilibrium Nanomorphology of Spinel Li4+xTi5O12

Marnix Wagemaker*†, Ernst R. H. van Eck‡, Arno P. M. Kentgens‡ and Fokko M. Mulder*†

J. Phys. Chem. B, 2009, 113 (1), pp 224–230
DOI: 10.1021/jp8073706

Abstract: Li4Ti5O12 spinel as Li-ion electrode material combines good capacity, excellent cycleability with a high rate capability. Although the potential of about 1.56 V vs Li is relatively high, these features make it the anode of choice for state of the art high power Li-ion batteries. Although the flat voltage profile reflects a two-phase reaction during lithiation, the small change in lattice parameters upon lithiation (“zero-strain” property) leads to a solid solution in equilibrium, as recently demonstrated with diffraction. In this study, the morphology and Li-ion mobility is studied by NMR spectroscopy leading to a more detailed picture, showing that the solid solution in Li4+xTi5O12 spinel should actually be described as domains with sizes less than 9 nm having either tetrahedral (8a) Li occupation or octahedral (16c) Li occupation. The abundant domain boundaries and the associated disorder appear to be responsible for the facile diffusion through the lattice, and hence these nm-sized domains are most likely the origin of the relative high rate capability of this material as electrode for Li-ion batteries. The small domain size, smaller than typical Debye lengths, makes that the material electrochemically behaves as a solid solution. As such, the results give insight in the fundamental properties of the “zero-strain” Li4Ti5O12 spinel material explaining the favorable Li-ion battery electrode properties on an atomic level.




Utilizing the Charge Field Effect on Amide 15N Chemical Shifts for Protein Structure Validation

Reto Bader*
J. Phys. Chem. B, 2009, 113 (1), pp 347–358

Abstract: Of all the nuclei in proteins, the nuclear magnetic resonance (NMR) chemical shifts of nitrogen are the theoretically least well understood. In this study, quantum chemical methods are used in combination with polarizable-continuum models in order to show that consideration of the effective electric field, including charge screening due to solvation, improves considerably the consistencies of statistical relationships between experimental and computed amide 15N shifts between various sets of charged and uncharged oligopeptides and small organic molecules. A single conversion scheme between shielding parameters from first principles using density functional theory (DFT) and experimental shifts is derived that holds for all classes of compounds examined here. This relationship is then used to test the accuracy of such 15N chemical shift predictions in the cyclic decapeptide antibiotic gramicidin S (GS). GS has previously been studied in great detail, both by NMR and X-ray crystallography. It adopts a well-defined backbone conformation, and hence, only a few discrete side chain conformational states need to be considered. Moreover, a charge-relay effect of the two cationic ornithine side chains to the protein backbone has been described earlier by NMR spectroscopy. Here, DFT-derived backbone amide nitrogen chemical shifts were calculated for multiple conformations of GS. Overall, the structural dynamics of GS is revisited in view of chemical shift behavior along with energetic considerations. Together, the study demonstrates proof of concept that 15N chemical shift information is particularly useful in the analysis and validation of protein conformational states in a charged environment.