6,122 research outputs found

    Strong interrelationship between anomalous electric-field induced lattice strain along non-polar direction and domain reorientation in pseudorhombohedral piezoelectric ceramic BiScO3-PbTiO3

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    The lattice strain and domain switching behaviour was investigated as a function of cyclic field and grain orientation for a pseudorhombohedral composition of the high Curie point piezoelectric system xBiScO3 - (1-x)PbTiO3 (x = 0.40) by in-situ electric field diffraction technique with high energy synchrotron x-rays. Along the field direction, the system exhibts five time large strain along 100 as compared to the 111 direction. A one-to-one correspondence between the 200 lattice strain and the 111 domain switching suggests a strong correlation between the two phenomena.Comment: 11 pages, 7 figure

    Low temperature dielectric relaxation in ordinary perovskite ferroelectrics: enlightenment from high-energy x-ray diffraction

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    Ordinary ferroelectrics exhibit a second order phase transition that is characterized by a sharp peak in the dielectric permittivity at a frequency-independent temperature. Furthermore, these materials show a low temperature dielectric relaxation that appears to be a common behavior of perovskite systems. Tetragonal lead zirconate titanate is used here as a model system in order to explore the origin of such an anomaly, since there is no consensus about the physical phenomenon involved in it. Crystallographic and domain structure studies are performed from temperature dependent synchrotron x-ray diffraction measurement. Results indicate that the dielectric relaxation cannot be associated with crystallographic or domain configuration changes. The relaxation process is then parameterized by using the Vogel–Fulcher–Tammann phenomenological equation. Results allow us to hypothesize that the observed phenomenon is due to changes in the dynamic behavior of the ferroelectric domains related to the fluctuation of the local polarization.Postprint (author's final draft

    PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins

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    Integral peroxisomal membrane proteins (PMPs) are synthesized in the cytoplasm and imported posttranslationally. Here, we demonstrate that PEX19 binds and stabilizes newly synthesized PMPs in the cytosol, binds to multiple PMP targeting signals (mPTSs), interacts with the hydrophobic domains of PMP targeting signals, and is essential for PMP targeting and import. These results show that PEX19 functions as both a chaperone and an import receptor for newly synthesized PMPs. We also demonstrate the existence of two PMP import mechanisms and two classes of mPTSs: class 1 mPTSs, which are bound by PEX19 and imported in a PEX19-dependent manner, and class 2 mPTSs, which are not bound by PEX19 and mediate protein import independently of PEX19

    PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins

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    PEX19 is a chaperone and import receptor for newly synthesized, class I peroxisomal membrane proteins (PMPs). PEX19 binds these PMPs in the cytoplasm and delivers them to the peroxisome for subsequent insertion into the peroxisome membrane, indicating that there may be a PEX19 docking factor in the peroxisome membrane. Here we show that PEX3 is required for PEX19 to dock at peroxisomes, interacts specifically with the docking domain of PEX19, and is required for recruitment of the PEX19 docking domain to peroxisomes. PEX3 is also sufficient to dock PEX19 at heterologous organelles and binds PEX19 via a conserved motif that is essential for this docking activity and for PEX3 function in general. Not surprisingly, transient inhibition of PEX3 abrogates class I PMP import but has no effect on class II PMP import or peroxisomal matrix protein import. Taken together, these results suggest that PEX3 plays a selective, essential, and direct role in PMP import as a docking factor for PEX19

    syn-Dispiro­[1,3-dioxolane-2,17′-penta­cyclo­[12.2.1.16,9.02,13.05,10]octa­decane-18′,2′′-[1,3]dioxolane]-7′,15′-diene

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    The title compound, C22H28O4, is composed of a central octa­decane ring and two spiro­[bicyclo­[2.2.1]hept[2]ene-7,2′-[1,3]dioxolane] units. This polycycle has pseudo twofold symmetry and the central cyclo­octane ring has a distorted boat configuration

    Particle Size on Respiratory Protection Provided by Two Types of N95 Respirators on Agricultural Settings

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    The objective of this study was to compare size-selective workplace protection factors (WPFs) of an N95 elastomeric respirator (ER) and an N95 filtering facepiece respirator (FFR) in agricultural environments. Twenty-five healthy farm workers ranging in age from 20 to 30 years voluntarily participated in the study. Altogether eight farms were included representing three different types: two horse farms, three pig barns, and three grain handling sites. Subjects wore the ER and FFR while performing their daily activities, such as spreading hay, feeding livestock, and shoveling. Aerosol concentrations in an optical particle size range of 0.7–10 µm were determined simultaneously inside and outside of the respirator during the first and last 15 minutes of a 60-minute experiment. For every subject, size-selective WPFs were calculated in one-minute intervals and averaged over 30 minutes. For the ER, geometric mean WPFs were 172, 321, 1013, 2097 and 2784 for particles of 0.7–1.0, 1.0–2.0, 2.0–3.0, 3.0–5.0, and 5.0–10.0 µm, respectively. Corresponding values for the FFR were 69, 127, 324, 893, and 1994. The 5th percentiles for the ER and FFR were higher than the Assigned Protection Factor of 10 and varied from 28 to 250 and from 16 to 225, respectively. The results show that the N95 ER and FFR tested in the study provided expected level of protection for workers on agricultural farms against particles ranging from 0.7 to 10 µm. The WPFs for the ER were higher than those for the FFR in all size ranges, and the WPFs for both respirators increased with increasing particle size
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