The aerodynamic performance of vehicles on a bridge deck depends on the local wind field, especially in a region near a bridge tower. This study was carried out on a large-scale (1: 20.4) truss girder, and wind tunnel tests were performed to determine how the wind fields were affected by the bridge tower in the presence of different wind barriers. The wind barrier parameters significantly affect the wind field. Wind barriers should be sufficiently high to provide a wide protection range and have relatively small porosities to reduce the wind speed. The opening form of the wind barrier should also be considered, where a circular-holed form reduces the wind speed and turbulence more than a horizontal-slatted form. The wind field is affected by structures and bridge towers on the deck. A turning point in the wind speed occurs at a measurement point near the bridge tower, and this point gradually moves upward towards lanes on the leeward side of the bridge. The equivalent wind speed is significantly reduced over a four-meter height range because of shadowing from the bridge tower and the wind barrier.
Based on main structural features of the high strength thrust bearing shells, ANSYS has been applied, in this paper, to establish a finite element model and simulate the combined stress and deformation of the high strength thrust bearing shells and connecting bolts between them.
Simulation results show that strength of high strength thrust bearing shell and the connecting bolts between the shells can meet the design requirement of the structure form with heavy thrust load and high strength.
Translocated intimin receptor (Tir) is an Escherichia coli-encoded protein that is transported into the host cell through a sophisticated bacterial type III secretion system (T3SS). Tir anchors the infected cell membrane twice using both its N- and C-termini from inside the host cytoplasm for signalling. It plays a key role in enterohemorrhagic Escherichia coli (EHEC) infection, attaching and effacing (A/E) lesions and intracellular signal transduction. Here, the overexpression, purification and crystallization of its N-terminal intracellular domain are reported. The crystal belonged to the orthorhombic space group I4122, with unit-cell parameters a = b = 59.79, c = 183.11 Å. The asymmetric unit contained one molecule, with a solvent content of 51% and a VM of 2.55 Å(3) Da(-1).
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