Experimental and theoretical N.M.R. studies of the coupling constants in seven isotopic ethyl fluorides

The N.M.R. spin-spin coupling constants and chemical shifts are reported for seven isotopically substituted ethyl fluorides. ¹H, ²H and ¹⁹F spectra have been observed and a consistent set of data obtained. Isotope effects are reported in ¹H and ¹⁹F spectra due to replacement of ¹H by ²H and ¹²C by ¹³C.

Using an accurate microwave structure of ethyl fluoride, CNDO and INDO calculations have been carried out, including dipolar and orbital terms. As independent options, configuration interaction between all single-excited states, variable radial electron distribution <r ^-3> and variable electron density at the site of nuclei, <s(0)²>, are included. Calculated values for all combinations of the options are given and a discussion of the results presented.     

Weakly Bound States of Polar Molecules in Bilayers

We investigate a system of two polarized molecules in a layered trap. The molecules reside in adjacent layers and interact purely via the dipole?Cdipole interaction. We determine the properties of the ground state of the system as a function of the dipole moment and polarization angle. A bound state is always present in the system and in the weak binding limit the bound state extends to a very large distance and shows universal behavior.     

Rapid quantitative measurements of proteomes by Fourier transform ion cyclotron resonance mass spectrometry.

The patterns of gene expression, post-translational modifications, protein/biomolecular interactions, and how these may be affected by changes in the environment, cannot be accurately predicted from DNA sequences. Approaches for proteome characterization are generally based upon mass spectrometric analysis of in-gel digested two dimensional polyacrylamide gel electrophoresis (2-D PAGE) separated proteins, allowing relatively rapid protein identification compared to conventional approaches. This technique, however, is constrained by the speed of the 2-D PAGE separations, the sensitivity limits intrinsic to staining necessary for protein visualization, the speed and sensitivity of subsequent mass spectrometric analyses for identification, and the limited ability for accurate quantitative measurements based on differences in spot intensity. We are presently developing alternative approaches for proteomics based upon the combination of fast capillary electrophoresis, or other suitable chromatographic separations, and the high mass accuracy and sensitivity obtainable with unique Fourier transform ion cyclotron resonance (FTICR) mass spectrometers available at our laboratory. Several approaches are presently being pursued; one based upon the analysis of intact proteins and the second upon approaches for global protein digestion and accurate peptide mass analysis. Quantitation of protein/peptide levels are based on using two or more stable-isotope labeled versions of proteomes which are combined to obtain precise quantitation of relative protein abundances. We describe the status of our efforts towards the development of a high-throughput proteomics capability and present initial results for application to several microorganisms and discuss our efforts for extending the developed capability to mammalian proteomes.     

Recent developments in the stereological analysis of particles

Recent developments in the stereological analysis of particles are reviewed. The trend has been towards methods which are applicable without specific assumptions about particle shape. Geometric samples of a local 3-d character are used. Stereological estimators of particle intensity, particle size distribution and particle interaction are presented and discussed.An earlier version of this article was presented at the Symposium on the Analysis of Statistical Information held in the Institute of Statistical Mathematics, Tokyo during December 5–8, 1989.     

Electron-microscopy studies of NaAlH4 with TiF3 additive: hydrogen-cycling effects

NaAlH₄ is a promising candidate material for hydrogen storage. Ti additives are effective in reducing the reaction temperatures and improving kinetics. In this work, the microstructure of NaAlH₄ with 2% TiF₃ has been studied in different conditions using a combination of transmission electron microscopy and scanning electron microscopy, both with energy-dispersive spectroscopic X-ray analysis. The effect of the additive on particle and grain size was examined after the initial ball-milling process and after 15 cycles. The additive has an uneven distribution in the sample after ball milling. Selected-area diffraction and high-resolution imaging confirmed the presence of TiF₃. This phase accounts for most of the Ti in the material at this stage and showed limited mixing with the alanate. The grain size within particles for TiF₃ is larger than for the alanate particles. Diffraction from the latter was dominated by metallic aluminium. After cycling, the TiF₃ has decomposed and energy-dispersive spectroscopic X-ray analysis maps showed some combination of Ti with the alanate phase. There is no significant change in the measurable grain size of the Al-containing alanate particles between the ball-milled and the 15-cycled samples, but more cycles result in agglomeration of the material. PACS 61.14.-x; 68.37.LP; 68.37.Hk