This paper reports on a series of shaking table tests on a full-scale flat-bottom steel silo filled with soft wheat, characterized by aspect ratio of around 0.9. The specimen was a 3.64-m diameter and 5.50-m high corrugated-wall cylindrical silo. Multiple sensors were used to monitor the static and dynamic response of the filled silo system, including accelerometers and pressure cells. Numerous unidirectional dynamic tests were performed consisting of random signals, sinusoidal inputs, and both artificial and real earthquake records. The objectives of this paper are (i) to provide a general overview of the whole experimental campaign and (ii) to present selected results obtained for the fixed-base configuration. The measured data were processed to assess the static pressures, the dynamic overpressures (related to the effective mass) and the accelerations of monitored points on the silo wall, and to identify the basic dynamic properties (fundamental frequency of vibration, damping ratio, dynamic amplification factors) of the filled silo. The main findings are discussed and compared with the This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
We have developed a novel method for linking proteins to DNA based on the HUH endonuclease family. HUH endonucleases are involved in replication of ssDNA in viruses and mobile bacterial plasmids. The HUH domain of the endonuclease nicks ssDNA at a specific sequence near the origin of replication, resulting in formation of a covalent phosphotyrosine intermediate between the DNA and catalytic tyrosine in the HUH protein. We have adapted these nucleases into small, soluble protein tags which robustly react with unmodified single-stranded DNA to form stable covalent bonds. We have shown that five of these proteins react with fully orthogonal DNA sequences and can be used for ''one-pot'', site-specific labeling of complex structures. Three tags have shown robust activity in cultured mammalian cells, allowing single-step DNA-based fluorescent labeling of fusion proteins. We believe that this technology can expand the possibilities for DNA nanotechnology, both in vitro and in cultured cells.
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