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In order to do the systematical dynamic modeling and analysis of the Ku-band 16 meter antenna satellite ground station used a satellite telecommunication, We calculated the eigenvalues of the the Ku-band 16 meter antenna structure, and used the SAP5, a large structure analysis software, to do the finite element calculation and analysis. The first ten band eigenvalues of the antenna structure were calculated; And the results showed that the minimum natural frequency was 2.075 Hz. Furthermore, based on National Military Standard, we measured the system frequency of the Ku-band 16 meter antenna satellite ground station and got the minimum natural frequency of 2.249 Hz. So there is quite good agreement between the theoretical minimum natural frequency (2.075 Hz) and the measuring minimum natural frequency (2.249 Hz). This shows that dynamic modeling and analysis of a large-scale antenna structure system is effective.

Appropriate preferences for light or dark conditions can be crucial for an animal's survival. Innate light preferences are not static in some animals, including the fruit fly Drosophila melanogaster, which prefers darkness in the feeding larval stage but prefers light in adulthood. To elucidate the neural circuit underlying light preference, we examined the neurons involved in larval phototactic behavior by regulating neuronal functions. Modulating activity of two pairs of isomorphic neurons in the central brain switched the larval light preference between photophobic and photophilic. These neurons were found to be immediately downstream of pdf-expressing lateral neurons, which are innervated by larval photoreceptors. Our results revealed a neural mechanism that could enable the adjustment of animals' response strategies to environmental stimuli according to biological needs.

RFWD3 has E3 ligase activity in vitro, but its in vivo function remains unknown. In this study we identified RFWD3 as a novel replication protein A (RPA)-associated protein. Using purified proteins, we observed a direct interaction between RPA2 and RFWD3. Further analysis showed that RFWD3 is recruited to stalled replication forks and co-localizes with RPA2 in response to replication stress. Moreover, RFWD3 is important for ATR-dependent Chk1 activation in response to replication stress. Upon replication stress, deletion of RPA2 binding region on RFWD3 impairs its localization to stalled replication forks and decreases Chk1 activation. Taken together, our results suggest that RFWD3 and RPA2 functionally interact and participate in replication checkpoint control.

We have demonstrated 1.5μm light emission from InAs quantum dots (QDs) capped with a thin GaAs layer. The extension of the emission wavelength can be assigned to the large QD height. We also investigate the effect of growth interruption on the PL properties and the shape of InAs QDs fabricated by migration-enhanced growth (MEG). Contrary to expectation, we observed a remarkable blueshift of the emission energy with the growth interruption in MEG mode. Detailed investigations reveal that the blueshift is related to the reduced island height with the growth interruption, which is confirmed by reflection high-energy electron diffraction (RHEED) patterns and atomic force microscopy (AFM) measurement results. Accordingly, the structure changes of the islands are interpreted in terms of thermodynamic and kinetic theories.

Human p66 alpha and p66 beta are two potent transcriptional repressors that interact with the methyl-CpG-binding domain proteins MBD2 and MBD3. An analysis of the molecular mechanisms mediating repression resulted in the identification of two major repression domains in p66 alpha and one in p66 beta. Both p66 alpha and p66 beta are SUMO-modified in vivo: p66a at two sites (Lys-30 and Lys-487) and p66 beta at one site (Lys-33). Expression of SUMO1 enhanced the transcriptional repression activity of Gal-p66 alpha and Gal-p66 beta. Mutation of the SUMO modification sites or using a SUMO1 mutant or a dominant negative Ubc9 ligase resulted in a significant decrease of the transcriptional repression of p66a and p66 beta. The Mi-2/NuRD components MBD3, RbAp46, RbAp48, and HDAC1 were found to bind to both p66 alpha and p66 beta in vivo. Most of the interactions were not affected by the SUMO site mutations in p66 alpha or p66 beta, with two exceptions. HDAC1 binding to p66 alpha was lost in the case of a p66 alpha K30R mutant, and RbAp46 binding was reduced in the case of a p66 beta K33R mutant. These results suggest that interactions within the Mi-2/NuRD complex as well as optimal repression are mediated by SUMOylation.