Dynamic model tracking design for low inertia, high speed permanent magnet ac motors

Permanent magnet a

Coverage-dependent adsorption sites for K/Cu(001) and Cs/Cu(001) determined by surface X-ray diffraction

Surface X-ray diffraction has been used to analyze in situ the room-temperature adsorption behaviour and the structure of K and Cs on Cu(100) at submonolayer coverages. Adsorption of K takes place in fourfold hollow sites up to coverages of about 0.25 monolayers (ML), where 1 ML corresponds to 1.53 × 1015 atoms/cm2. At higher coverages the formation of a quasi-hexagonal incommensurate adlayer is observed. In contrast, for Cs adsorption we observe from the very beginning the formation of the quasi-hexagonal structure up to the completion of the adlayer at about 0.30 ML. For K adsorption in the hollow sites we determine an adsorption height, d = 2.25(15) Å, corresponding to an effective K radius of reff = 1.6(1) Å close to the ionic radius of 1.33 Å. We do not observe a change in the effective radius as a function of coverage. For the quasi-hexagonal Cs structure we find an (average) adsorption height d = 2.94 Å corresponding to an effective radius of reff = 2.18 and 1.93 Å, for the limiting ca hollow- and bridge-site adsorption, respectively. The analysis of the superlattice reflections corresponding to the quasi-hexagonal incommensurate structures indicated that the K adlayer is strongly modulated. The first Fourier component of the substrate-induced modulation was determined to u01 = 1.29(3) Å. In contrast, for Cs/Cu(001) static modulation is much less important (u01 0.2 Å). Variation of the Cs adlayer density by changing the substrate temperature allows continuous expansion and contraction of the adsorbate unit cell. No commensurate-incommensurate transition has been observed

The structure of K- and Cs-monolayers on Cu(0 0 1): diffraction experiments far from the Bragg point

The intensity analysis along the crystal truncation rods has been used to analyse in situ the adsorption behaviour and the structure of K and Cs on Cu(0 0 1) at submonolayer coverages and room temperature. Up to about 0.25 ML K atoms adsorb in hollow sites followed by formation of a quasihexagonal superstructure. In contrast, for Cs adsorption the data can be interpreted by the formation of quasihexagonal Cs islands that grow with increasing coverage. For K an effective radius of 1.6(1) Å independent of coverage is determined. For Cs we fnd d = 2.1 (1) Å after formation of the quasihexagonal superstructure

X-ray structure analysis of the InSb ( )-(3 × 3) reconstruction

The (3 × 3) reconstruction of the InSb( ) surface has been analysed using grazing incidence X-ray diffraction. The reconstruction is characterized by hexamers above a complete InSb double-layer centred around an Sb atom. No vacancies are found in the structure as predicted theoretically. The results agree with scanning tunnelling microscopy measurements

Unmasking features of the auto-epitope essential for β(1)-adrenoceptor activation by autoantibodies in chronic heart failure

AIMS: Chronic heart failure (CHF) can be caused by autoantibodies stimulating the heart via binding to first and/or second extracellular loops of cardiac β(1)-adrenoceptors. Allosteric receptor activation depends on conformational features of the autoantibody binding site. Elucidating these features will pave the way for the development of specific diagnostics and therapeutics. Our aim was (i) to fine-map the conformational epitope within the second extracellular loop of the human β(1)-adrenoceptor (β(1) EC(II)) that is targeted by stimulating β(1)-receptor (auto)antibodies and (ii) to generate competitive cyclopeptide inhibitors of allosteric receptor activation, which faithfully conserve the conformational auto-epitope. METHODS AND RESULTS: Non-conserved amino acids within the β(1) ECII loop (compared with the amino acids constituting the ECII loop of the β(2)-adrenoceptor) were one by one replaced with alanine; potential intra-loop disulfide bridges were probed by cysteine-serine exchanges. Effects on antibody binding and allosteric receptor activation were assessed (i) by (auto)antibody neutralization using cyclopeptides mimicking β(1) ECII ± the above replacements, and (ii) by (auto)antibody stimulation of human β(1)-adrenoceptors bearing corresponding point mutations. With the use of stimulating β(1)-receptor (auto)antibodies raised in mice, rats, or rabbits and isolated from exemplary dilated cardiomyopathy patients, our series of experiments unmasked two features of the β(1) ECII loop essential for (auto)antibody binding and allosteric receptor activation: (i) the NDPK(211-214) motif and (ii) the intra-loop disulfide bond C(209)↔C(215). Of note, aberrant intra-loop disulfide bond C(209)↔C(216) almost fully disrupted the functional auto-epitope in cyclopeptides. CONCLUSIONS: The conformational auto-epitope targeted by cardio-pathogenic β(1)-receptor autoantibodies is faithfully conserved in cyclopeptide homologues of the β(1) EC(II) loop bearing the NDPK(211-214) motif and the C(209)↔C(215) bridge while lacking cysteine C(216). Such molecules provide promising tools for novel diagnostic and therapeutic approaches in β(1)-autoantibody-positive CHF

Antibaryons in massive heavy ion reactions: Importance of potentials

In the framework of RQMD we investigate antiproton observables in massive heavy ion collisions at AGS energies and compare to preliminary results of the E878 collaboration. We focus here on the considerable influence of the *real* part of an antinucleon--nucleus optical potential on the antiproton momentum spectra

Atp bioluminescence for rapid and selective detection of bacteria and yeasts in wine

Microbial contamination may represent a loss of money for wine producers as several defects can arise due to a microorganism’s growth during storage. The aim of this study was to implement a bioluminescence assay protocol to rapidly and simultaneously detect bacteria and yeasts in wines. Different wines samples were deliberately contaminated with bacteria and yeasts at different concentrations and filtered through two serial filters with decreasing mesh to separate bacteria and yeasts. These were resuscitated over 24 h on selective liquid media and analyzed by bioluminescence assay. ATP measurements discriminated the presence of yeasts and bacteria in artificially contaminated wine samples down to 50 CFU/L of yeasts and 1000 CFU/L of bacteria. The developed protocol allowed to detect, rapidly (24 h) and simultaneously, bacteria and yeasts in different types of wines. This would be of great interest for industries, for which an early detection and discrimination of microbial contaminants would help in the decision‐making proces

Photosystem II core phosphorylation and photosynthetic acclimation require two different protein kinases

Illumination changes elicit modifications of thylakoid proteins and reorganization of the photosynthetic machinery. This involves, in the short term, phosphorylation of photosystem II (PSII) and light-harvesting (LHCII) proteins. PSII phosphorylation is thought to be relevant for PSII turnover1,2, whereas LHCII phosphorylation is associated with the relocation of LHCII and the redistribution of excitation energy (state transitions) between photosystems3,4. In the long term, imbalances in energy distribution between photosystems are counteracted by adjusting photosystem stoichiometry5,6. In the green alga Chlamydomonas and the plant Arabidopsis, state transitions require the orthologous protein kinases STT7 and STN7, respectively7,8. Here we show that in Arabidopsis a second protein kinase, STN8, is required for the quantitative phosphorylation of PSII core proteins. However, PSII activity under high-intensity light is affected only slightly in stn8 mutants, and D1 turnover is indistinguishable from the wild type, implying that reversible protein phosphorylation is not essential for PSII repair. Acclimation to changes in light quality is defective in stn7 but not in stn8 mutants, indicating that short-term and long-term photosynthetic adaptations are coupled. Therefore the phosphorylation of LHCII, or of an unknown substrate of STN7, is also crucial for the control of photosynthetic gene expressio