| 1. |
- Fröjdh, Erik, et al.
(författare)
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Timepix3 : first measurements and characterization of a hybrid-pixel detector working in event driven mode
- 2015
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Ingår i: Journal of Instrumentation. - 1748-0221 .- 1748-0221. ; 10
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Tidskriftsartikel (refereegranskat)abstract
- Timepix3 is a hybrid pixel detector readout chip. It features a data driven readout mode where the chip sends out a data packet containing pixel coordinate, time over threshold and time of arrival immediately after the hit is processed by the pixel. The maximum hit rate is 40 Mhits/cm(2)/s with a minimum time step in the arrival time measurement of 1.56 ns. The pixel matrix consist of 256 x 256 square pixels at a 55 m m pitch and the pixel front end noise is 61 e(-) RMS. In this paper we present the first radiation measurements with Timepix3 bump bonded to a 300 m m thick silicon sensor. The chip is calibrated per pixel, using internal test pulses and the calibration is verified using X-ray fluorescence. The energy resolution, threshold dispersion and gain dispersion is measured. The energy resolution in time over threshold mode under normal operation conditions is 4.07 keV FWHM at 59.5 keV. At 10.5 keV an energy resolution of 0.72 keV FWHM was achieved in photon counting mode and in time over threshold mode, by optimizing the energy response, we achieved a 1.38 keV FWHM. We also investigate the time walk and present first results on using the time information for track reconstruction.
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| 2. |
- Graf, L., et al.
(författare)
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The Role of Structural Flexibility and Stability in the Interaction of Serine Proteases with their Inhibitors
- 2015
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Ingår i: Current Protein & Peptide Science. - 1389-2037. ; 16:6, s. 521-531
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Forskningsöversikt (refereegranskat)abstract
- Serine proteases and their natural inhibitors have long been served as excellent models for studying (primary, secondary and tertiary) structure - activity relationships of biologically interacting proteins. As protein flexibility has been accepted as a "fourth dimension" of the protein structure, its contribution to the binding process has gained much interest. In this article we review extreme cases of serine protease interactions with canonical serine protease inhibitors that provide unique insights into the dynamics of protein-protein interactions. The major conclusions of our review article are: a) taxon-specific inhibitory effects of two highly homologous protease inhibitors from Schistocerca gregaria (SGCI and SGTI), as investigated by H/D exchange experiments and NMR spectroscopy, are due to their differential flexibilities, b) stabilities of some protease and inhibitor complexes, the wide-spread and increased flexibility of some segments in the protein-protein complexes, as studied by X-ray crystallography and NMR-spectroscopy, appear to be proportional to the physical stability of the complex.
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