937 resultados para ENERGY-ABSORBING STRUCTURE
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The Bi-directional Evolutionary Structural Optimisation (BESO) method is a numerical topology optimisation method developed for use in finite element analysis. This paper presents a particular application of the BESO method to optimise the energy absorbing capability of metallic structures. The optimisation objective is to evolve a structural geometry of minimum mass while ensuring that the kinetic energy of an impacting projectile is reduced to a level which prevents perforation. Individual elements in a finite element mesh are deleted when a prescribed damage criterion is exceeded. An energy absorbing structure subjected to projectile impact will fail once the level of damage results in a critical perforation size. It is therefore necessary to constrain an optimisation algorithm from producing such candidate solutions. An algorithm to detect perforation was implemented within a BESO framework which incorporated a ductile material damage model.
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We demonstrate that commonly face-centered cubic (fcc) metallic nanowires can be stabilized in hexagonal structures even when their surface energy contribution is relatively small. With a modified electrochemical growth process, we have grown purely single-crystalline 4H silver nanowires (AgNWs) of diameters as large as 100 nm within nanoporous anodic alumina and polycarbonate templates. The growth process is not limited by the/Ag Nernst equilibrium potential, and time-resolved imaging with high-resolution transmission electron microscopy (TEM) indicates a kinematically new mechanism of nanowire growth. Most importantly, our experiments aim to separate the effects of confinement and growth conditions on the crystal structure of nanoscale systems.
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There are many well-known examples of proteins with low sequence similarity, adopting the same structural fold. This aspect of sequence-structure relationship has been extensively studied both experimentally and theoretically, however with limited success. Most of the studies consider remote homology or ``sequence conservation'' as the basis for their understanding. Recently ``interaction energy'' based network formalism (Protein Energy Networks (PENs)) was developed to understand the determinants of protein structures. In this paper we have used these PENs to investigate the common non-covalent interactions and their collective features which stabilize the TIM barrel fold. We have also developed a method of aligning PENs in order to understand the spatial conservation of interactions in the fold. We have identified key common interactions responsible for the conservation of the TIM fold, despite high sequence dissimilarity. For instance, the central beta barrel of the TIM fold is stabilized by long-range high energy electrostatic interactions and low-energy contiguous vdW interactions in certain families. The other interfaces like the helix-sheet or the helix-helix seem to be devoid of any high energy conserved interactions. Conserved interactions in the loop regions around the catalytic site of the TIM fold have also been identified, pointing out their significance in both structural and functional evolution. Based on these investigations, we have developed a novel network based phylogenetic analysis for remote homologues, which can perform better than sequence based phylogeny. Such an analysis is more meaningful from both structural and functional evolutionary perspective. We believe that the information obtained through the ``interaction conservation'' viewpoint and the subsequently developed method of structure network alignment, can shed new light in the fields of fold organization and de novo computational protein design.
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National Highway Traffic Safety Administration, Washington, D.C.
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Connecticut Department of Transportation, Bureau of Planning and Research, Wethersfield
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National Highway Traffic Safety Administration, Washington, D.C.
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National Highway Traffic Safety Administration, Washington, D.C.
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National Highway Traffic Safety Administration, Washington, D.C.