6 research outputs found

    Meter-scale spark X-ray spectrumstatistics

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    X-ray emission by sparks implies bremsstrahlung from a population of energetic electrons, but the details of this process remain a mystery. We present detailed statistical analysis of X-ray spectra detected by multiple detectors during sparks produced by 1 MV negative high-voltage pulses with 1 μ\mus risetime. With over 900 shots, we statistically analyze the signals, assuming that the distribution of spark X-ray fluence behaves as a power law and that the energy spectrum of X-rays detectable after traversing \sim2 m of air and a thin aluminum shield is exponential. We then determine the parameters of those distributions by fitting cumulative distribution functions to the observations. The fit results match the observations very well if the mean of the exponential X-ray energy distribution is 86 ±\pm 7 keV and the spark X-ray fluence power law distribution has index -1.29 ±\pm 0.04 and spans at least 3 orders of magnitude in fluence

    Fluorescence correlation spectroscopy of the binding of nucleotide excision repair protein XPC-hHr23B with DNA substrates

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    The interaction of the nucleotide excision repair (NER) protein dimeric complex XPC-hHR23B, which is implicated in the DNA damage recognition step, with three Cy3.5 labeled 90-bp double-stranded DNA substrates (unmodified, with a central unpaired region, and cholesterol modified) and a 90-mer single-strand DNA was investigated in solution by fluorescence correlation spectroscopy. Autocorrelation functions obtained in the presence of an excess of protein show larger diffusion times (τ d) than for free DNA, indicating the presence of DNA-protein bound complexes. The fraction of DNA bound (θ), as a way to describe the percentage of protein bound to DNA, was directly estimated from FCS data. A significantly stronger binding capability for the cholesterol modified substrate (78% DNA bound) than for other double-stranded DNA substrates was observed, while the lowest affinity was found for the single-stranded DNA (27%). This is in accordance with a damage recognition role of the XPC protein. The similar affinity of XPC for undamaged and 'bubble' DNA sub

    Capillary Electrophoresis for the Analysis of Biopolymers

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