We report the applicability of ZrO 2 /ZnO impregnated onto a variety of MgO:SiO 2 materials as heterogeneous catalysts for the conversion of ethanol to 1,3-butadiene. The selectivity to 1,3-butadiene is affected by the ratio of the basic MgO to the acidic SiO 2 , with higher selectivities being observed as the mole fraction of MgO increases. The catalysts have been characterised by SEM, XPS, pXRD, BET surface area measurements and 29 Si solid-state NMR spectroscopy.

High-resolution ultrasonic spectroscopy was applied for real-time monitoring of the heat-induced denaturation and aggregation processes in aqueous solutions of β-lactoglobulin. The temperature profiles for the ultrasonic velocity and attenuation in the frequency range from 4 MHz to 16 MHz were measured during heating and cooling cycles, 35 • C to 120 • C to 35 • C, with different heating and cooling rates. Two processes were identified in the heating profiles: transition to the molten globular state followed by formation of protein aggregates. Both processes are accompanied by a decrease in the ultrasonic velocity and an increase in compressibility. The ultrasonic attenuation did not show a significant change during the transition to the molten globule but increased significantly during aggregation. The diameter of the aggregates (calculated from ultrasonic attenuation) was of the order of 100 nm and depended on the pH and the heating rate. Variation of pH from 6.0 to 7.5 had a pronounced effect on the size of protein aggregates. Some effect of pH on the intrinsic properties of aggregates was also detected.

Fluorescence Resonance Energy Transfer (FRET) was used to study protein structures within soluble oligomer intermediates of amyloid and non-amyloid aggregates. Three protein aggregation systems were studied using fluorescence donor and acceptor near the N and C terminus:(1) Alzheimer's Ab 1-40 peptide.(2) 20-residue polyglutamine K 2 Q 16 K 2 .(3) 20-residue polyglutamic acid E 20 . (non-amyloid) The aggregation of each peptide showed different conformational changes: Ab 1-40 partially compacted into a structure consistent with solid-state NMR structures, K 2 Q 16 K 2 extended to form b-sheets, and E 20 compacted heavily into b-hairpins. However, based on donor-acceptor distances, soluble oligomers conformations of all three peptides show a remarkable degree of similarity to their monomeric precursors, albeit with a slightly expanded conformation for Ab 1-40 and E 20 . These findings support assembly models of small soluble oligomers which largely consist of monomer-like structures, with some increase in a-helical content for Ab 1-40 . These donor-acceptor distances are used to directly assess the accuracy of different molecular dynamics force fields in the study of these soluble oligomers.