3,604 research outputs found

    Classifying RI/FS Costs Under a Policy of Comprehensive General Liability Insurance: Indemnity or Defense

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    On the Formation Height of the SDO/HMI Fe 6173 Doppler Signal

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    The Helioseismic and Magnetic Imager (HMI) onboard the Solar Dynamics Observatory (SDO) is designed to study oscillations and the mag- netic field in the solar photosphere. It observes the full solar disk in the Fe I absorption line at 6173\AA . We use the output of a high-resolution 3D, time- dependent, radiation-hydrodynamic simulation based on the CO5BOLD code to calculate profiles F({\lambda},x,y,t) for the Fe I 6173{\AA} line. The emerging profiles F({\lambda},x,y,t) are multiplied by a representative set of HMI filter transmission profiles R_i({\lambda},1 \leq i \leq 6) and filtergrams I_i(x,y,t;1 \leq i \leq 6) are constructed for six wavelengths. Doppler velocities V_HMI(x,y,t) are determined from these filtergrams using a simplified version of the HMI pipeline. The Doppler velocities are correlated with the original velocities in the simulated atmosphere. The cross- correlation peaks near 100 km, suggesting that the HMI Doppler velocity signal is formed rather low in the solar atmosphere. The same analysis is performed for the SOHO/MDI Ni I line at 6768\AA . The MDI Doppler signal is formed slightly higher at around 125 km. Taking into account the limited spatial resolution of the instruments, the apparent formation height of both the HMI and MDI Doppler signal increases by 40 to 50 km. We also study how uncertainties in the HMI filter-transmission profiles affect the calculated velocities.Comment: 15 pages, 11 Figure

    Thermodynamics of Heat Shock Response

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    Production of heat shock proteins are induced when a living cell is exposed to a rise in temperature. The heat shock response of protein DnaK synthesis in E.coli for temperature shifts from temperature T to T plus 7 degrees, respectively to T minus 7 degrees is measured as function of the initial temperature T. We observe a reversed heat shock at low T. The magnitude of the shock increases when one increase the distance to the temperature T023oT_0 \approx 23^o, thereby mimicking the non monotous stability of proteins at low temperature. Further we found that the variation of the heat shock with T quantitatively follows the thermodynamic stability of proteins with temperature. This suggest that stability related to hot as well as cold unfolding of proteins is directly implemented in the biological control of protein folding. We demonstrate that such an implementation is possible in a minimalistic chemical network.Comment: To be published in Physical Review Letter
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