130,552 research outputs found
Engage with the limit. The open space as design element to enhance and reconnect fringes
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Functional characterization of a tyrosinase gene from the oomycete Saprolegnia parasitica by RNAi silencing
No full textAbstract not availableMarcia Saraiva, Irene de Bruijn, Laura Grenville-Briggs, Debbie McLaggan, Ariane Willems, Vincent Bulone, Pieter van Wes
Degalatosylated xyloglucan hydrogels: influence of irradiation conditions on physico-chemical properties and structure
No full textIrreversible gelation of thermally unfolded proteins:structural and mechanical properties of lysozyme aggregates
No full textThe formation of protein aggregates is important in many fields of life science and technology. The morphological and mechanical properties of protein solutions depend upon the molecular conformation and thermodynamic and environmental conditions. Non-native or unfolded proteins may be kinetically trapped into irreversible aggregates and undergo precipitation or gelation. Here, we study the thermal aggregation of lysozyme in neutral solutions. We characterise the irreversible unfolding of lysozyme by differential scanning calorimetry. The structural properties of aggregates and their mechanisms of formation with the eventual gelation are studied at high temperature by spectroscopic, rheological and scattering techniques. The experiments show that irreversible micron-sized aggregates are organised into larger clusters according to a classical mechanism of diffusion and coagulation, which leads to a percolative transition at high concentrations. At a smaller length scale, optical and atomic force microscopy images reveal the existence of compact aggregates, which are the origin of the aggregation irreversibility
Temperature-responsive degalactosylated xyloglucans as nanocarriers for the sustained release of hydrophobic drugs
No full textDiscrimination of hand fresh squeezed and commercial grapefruit juices by electronic nose.
No full textThe structure of model membranes studied by vibrational sum frequency spectroscopy
No full textThe structure and order of insoluble Langmuir monolayers consisting of 1,2-distearoyl-sn-glycero-3-phosphatidylcholine (DSPC or 18:0 PC) and the surrounding water molecules have been investigated by vibrational sum frequency spectroscopy (VSFS). At surface pressures of 1, 15, and 57 mN/m corresponding to molecular areas of 53, 50, and 43 Å2, respectively, the DSPC molecules formed a well ordered film. Both the VSF signal from the methyl stretching vibrations of the lipid and the surrounding water increased with enhanced surface pressure, as a result of the higher surface density and increased order of the system. Water molecules hydrating the polar parts of the headgroup and in close contact to the hydrocarbon groups of the lipid were observed in all three polarization combinations of the laser beams, and distinguished by their different vibrational frequencies.Jonathan F. D. Liljeblad, Mark W. Rutland, Vincent Bulone, C. Magnus Johnso
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