The MERSADE (European Union) project: testing procedures and environmental impact for the safe storage of liquid mercury in the Almadén district, Spain.

The MERSADE Project (LIFE--European Union) tested the Las Cuevas decommissioned mining complex (Almadén mercury district, Spain) as a potential site for the installation of a future European prototype safe deposit of surplus mercury from industrial activities. We here present the results of a baseline study on the distribution of mercury in soils and air in the Las Cuevas complex and surrounding areas, and show the results of a plume contamination model using the ISC-AERMOD software. Despite restoration works carried out in 2004, the Las Cuevas complex can still be regarded as hotspot of mercury contamination, with large anomalies above 800 microg g(-1) Hg (soils) and 300 ng Hg m(-3) (air). In the case of soils, high, and persistent concentrations above 26 microg g(-1) Hg extend well beyond the complex perimeter for more than 2 km. These concentrations are about three orders of magnitude above world baselines. The same applies to mercury in air, with high concentrations above 300 ng Hg m(-3) inside the perimeter, which nonetheless fade away in a few hundred meters. Air contamination modelling (Hg gas) predicts formation of a NW-SE oriented narrow plume extending for a few hundred meters from the complex perimeter. The geographic isolation of Las Cuevas and its mining past make the complex an ideal site for mercury stocking. The only potential environmental hazards are the raising of livestock only a few hundred meters away from the complex and flash floods.

Small volume flow probe for automated direct-injection NMR analysis: design and performance.

A detailed characterization of an NMR flow probe for use in direct-injection sample analysis is presented. A 600-MHz, indirect detection NMR flow probe with a 120-microl active volume is evaluated in two configurations: first as a stand-alone small volume probe for the analysis of static, nonflowing solutions, and second as a component in an integrated liquids-handling system used for high-throughput NMR analysis. In the stand-alone mode, (1)H lineshape, sensitivity, radiofrequency (RF) homogeneity, and heat transfer characteristics are measured and compared to conventional-format NMR probes of related design. Commonly used descriptive terminology for the hardware, sample regions, and RF coils are reviewed or defined, and test procedures developed for flow probes are described. The flow probe displayed general performance that is competitive with standard probes. Key advantages of the flow probe include high molar sensitivity, ease of use in an automation setup, and superior reproducibility of magnetic field homogeneity which enables the practical implementation of 1D T2-edited analysis of protein-ligand interactions.

1H NMR of A beta amyloid peptide congeners in water solution. Conformational changes correlate with plaque competence.

To begin to examine the structural basis for the deposition of soluble A beta amyloid peptide onto senile plaques in Alzheimer's disease, we have prepared A beta congeners and measured their activity in an in vitro plaque growth assay. The N-terminal fragment, A beta (1-28)-OH, was inactive at all pH values tested. While the central fragment, A beta (10-35)-NH2, and the full length peptide, A beta (1-40)-OH, were inactive below pH 4, both were active (plaque competent) between pH 5 and 9. The active and inactive fragments were studied by nuclear magnetic resonance spectroscopy in water at submillimolar concentrations at pH 2.1 and 5.6. Changes in chemical shifts, coupling constants, and nuclear Overhauser enhancements indicate a pH dependent folding transition in A beta (10-35)-NH2 as it becomes active. The conformation of the active fragment is not helical, and preliminary data indicate the presence of several turns and at least two short strands. In contrast, the inactive fragment A beta (1-28)-OH did not undergo a similar folding transition. Earlier nuclear magnetic resonance studies of amyloid peptides in fluorinated alcohols or detergent micelles at low pH described a helical conformation and proposed a helix to sheet transition in plaque formation; the present study demonstrates that no such conformations are present in water under conditions where the peptides can adhere to authentic amyloid plaques.