PubMed · 13456670
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H PIEPER, R WAGNER. 1957. [Thermically compensated manometer].. https://pubmed.ncbi.nlm.nih.gov/13456670/
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Monodispersed ZnO nanoparticles are easily prepared by the thermolysis of EtZnO(i)Pr as a single molecular precursor and TOPO without any extra solvent as well as any oxygen source.
A miniature broadband light source is a critical element in a spectrophotometric microsystem. The design, fabrication, and characterization of a highly stable, miniature broadband light source that comprises filaments of single-crystal silicon are presented. Electrical current versus voltage and radiant emittance spectra under constant voltage bias are measured and related to filament dimensions. A maximum stable operating temperature for these filaments is estimated to be 1200 K. Resistance drift is demonstrated to be less than 0.5% over a 10-h period of continuous operation with visible incandescence. Emittance spectra of a multifilament array, measured at three different electrical biases, are presented and shown to compare well with theoretical blackbody radiation spectra. A continuous, total radiated power of 10.7 mW was achieved with a 1 mm x 1 mm filament array with peak emittance at lambda=2.7 micrometers.
The effect of hydrostatic pressure on the secondary structure of recombinant human interferon-gamma (rhIFN-gamma) and its biologically inactive truncated form rhIFN-Delta C15 has been studied using Fourier-transform IR (FTIR) spectroscopy. In situ observation of the pressure-induced changes using the diamond anvil cell shows that the alpha-helical structure is mainly transformed into disordered structure at high pressure. Increasing pressure also induces the formation of a gel. Addition of 0.5 M MgCl(2) significantly reduces the pressure stability. Releasing the pressure below 300 MPa results in the formation of intermolecular antiparallel beta-sheets, which is seldom observed. This suggests that the intermolecular beta-sheet of rhIFN-gamma is stabilized by electrostatic interactions that are disrupted at high pressure. For comparison we also studied the effect of temperature. Temperature-induced changes reflect extensive transformation of alpha-helical structure into intermolecular antiparallel beta-sheet, as is usually observed for most proteins.