Integrated Experimental, Atomistic, and Microstructurally Based Finite Element Investigation of the Dynamic Compressive Behavior of 2139 Aluminum

The objective of this study was to identify the microstructural mechanisms related to the high strength and ductile behavior of 2139-Al, and how dynamic conditions would affect the overall behavior of this alloy. Three interrelated approaches, which span a spectrum of spatial and temporal scales, were used: (i) The mechanical response was obtained using the split Hopkinson pressure bar, for strain-rates ranging from 1.0×10^(−3) s to 1.0×10^4 s^(−1). (ii) First principles density functional theory calculations were undertaken to characterize the structure of the interface and to better understand the role played by Ag in promoting the formation of the Ω phase for several Ω-Al interface structures. (iii) A specialized microstructurally based finite element analysis and a dislocation-density based multiple-slip formulation that accounts for an explicit crystallographic and morphological representation of Ω and Θ' precipitates and their rational orientation relations were conducted. The predictions from the microstructural finite element model indicated that the precipitates continue to harden and also act as physical barriers that impede the matrix from forming large connected zones of intense plastic strain. As the microstructural FE predictions indicated, and consistent with the experimental observations, the combined effects of Θ' and Ω, acting on different crystallographic orientations, enhance the strength and ductility, and reduce the susceptibility of 2139-Al to shear strain localization due to dynamic compressive loads

Crystal Structure of a Novel Esterase Rv0045c from Mycobacterium tuberculosis

There are at least 250 enzymes in Mycobacterium tuberculosis (M. tuberculosis) involved in lipid metabolism. Some of the enzymes are required for bacterial survival and full virulence. The esterase Rv0045c shares little amino acid sequence similarity with other members of the esterase/lipase family. Here, we report the 3D structure of Rv0045c. Our studies demonstrated that Rv0045c is a novel member of α/β hydrolase fold family. The structure of esterase Rv0045c contains two distinct domains: the α/β fold domain and the cap domain. The active site of esterase Rv0045c is highly conserved and comprised of two residues: Ser154 and His309. We proposed that Rv0045c probably employs two kinds of enzymatic mechanisms when hydrolyzing C-O ester bonds within substrates. The structure provides insight into the hydrolysis mechanism of the C-O ester bond, and will be helpful in understanding the ester/lipid metabolism in M. tuberculosis

Two-dimensional fiber-optic vector vibroscope using only one multi-mode tilted fiber grating

Orientation-recognized two-dimensional vibration sensor based on a polarization-controlled cladding-to-core recoupling is demonstrated experimentally. A compact structure in which a short section of multi-mode fiber stub containi