986 resultados para NEW RECORD


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The two-country monetary model is extended to include a consumption externality with habit persistence. The model is simulated using the artificial economy methodology. The 'puzzles' in the forward market are re-examined. The model is able to account for: (a) the low volatility of the forward discount; (b) the higher volatility of expected forward speculative profit; (c) the even higher volatility of the spot return; (d) the persistence in the forward discount; (e) the martingale behavior of spot exchange rates; and (f) the negative covariance between the expected spot return and expected forward speculative profit. It is unable to account for the forward market bias because the volatility of the expected spot return is too large relative to the volatility of the expected forward speculative profit.

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No abstract.

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The conceptual design of a new electron beam ion trap primarily intended for the study of electron-ion interactions is outlined along with some preliminary predictions regarding its capabilities. (C) 2003 Elsevier Science B.V. All rights reserved.

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Electron beam trajectory simulations have been performed to design a new electron beam ion trap. The design of the magnet and electrode structures was optimized based on the results of the simulations. (C) 2003 Elsevier Science B.V. All rights reserved.

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An electron beam ion trap ( EBIT) has been designed and is currently under construction for use in atomic physics experiments at the Queen's University, Belfast. In contrast to traditional EBITs where pairs of superconducting magnets are used, a pair of permanent magnets will be used to compress the electron beam. The permanent magnets have been designed in conjunction with bespoke vacuum ports to give unprecedented access for photon detection. Furthermore, the bespoke vacuum ports facillitate a versatile, reconfigurable trap structure able to accommodate various in-situ detectors and in-line charged particle analysers. Although the machine will have somewhat lower specifications than many existing EBITs in terms of beam current density, it is hoped that the unique features will facilitate a number of hitherto impossible studies involving interactions between electrons and highly charged ions. In this article the new machine's design is outlined along with some suggestions of the type of process to be studied once the construction is completed.

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The past few years have seen remarkable progress in the development of laser-based particle accelerators. The ability to produce ultrabright beams of multi-megaelectronvolt protons routinely has many potential uses from engineering to medicine, but for this potential to be realized substantial improvements in the performances of these devices must be made. Here we show that in the laser-driven accelerator that has been demonstrated experimentally to produce the highest energy protons, scaling laws derived from fluid models and supported by numerical simulations can be used to accurately describe the acceleration of proton beams for a large range of laser and target parameters. This enables us to evaluate the laser parameters needed to produce high-energy and high-quality proton beams of interest for radiography of dense objects or proton therapy of deep-seated tumours.

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We report on our findings of the bright, pulsating, helium atmosphere white dwarf GD 358, based on time-resolved optical spectrophotometry. We identify 5 real pulsation modes and at least 6 combination modes at frequencies consistent with those found in previous observations. The measured Doppler shifts from our spectra show variations with amplitudes of up to 5.5 km s-1 at the frequencies inferred from the flux variations. We conclude that these are variations in the line-of-sight velocities associated with the pulsational motion. We use the observed flux and velocity amplitudes and phases to test theoretical predictions within the convective driving framework, and compare these with similar observations of the hydrogen atmosphere white dwarf pulsators (DAVs). The wavelength dependence of the fractional pulsation amplitudes (chromatic amplitudes) allows us to conclude that all five real modes share the same spherical degree, most likely, l=1. This is consistent with previous identifications based solely on photometry. We find that a high signal-to-noise mean spectrum on its own is not enough to determine the atmospheric parameters and that there are small but significant discrepancies between the observations and model atmospheres. The source of these remains to be identified. While we infer Teff =24 kK and log g ~ 8.0 from the mean spectrum, the chromatic amplitudes, which are a measure of the derivative of the flux with respect to the temperature, unambiguously favour a higher effective temperature, 27 kK, which is more in line with independent determinations from ultra-violet spectra.

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Phosphonopyruvate (P-pyr) hydrolase (PPH), a member of the phosphoenolpyruvate (PEP) mutase/isocitrate lyase (PEPM/ICL) superfamily, hydrolyzes P-pyr and shares the highest sequence identity and functional similarity with PEPM. Recombinant PPH from Variovorax sp. Pal2 was expressed in Escherichia coli and purified to homogeneity. Analytical gel filtration indicated that the protein exists in solution predominantly as a tetramer. The PPH pH rate profile indicates maximal activity over a broad pH range.The steady-state kinetic constants determined for a rapid equilibrium ordered kinetic mechanism with Mg+2 binding first (Kd =140 ± 40 M), are kcat = 105 ± 2 s-1 and P-pyr Km = 5 ± 1 M. PEP (slow substrate kcat = 2 × 10-4 s-1), oxalate, and sulfopyruvate are competitive inhibitors with Ki values of 2.0 ± 0.1 mM, 17 ± 1 M, and 210 ± 10 M, respectively. Three PPH crystal structures have been determined, that of a ligand-free enzyme, the enzyme bound to Mg2+ and oxalate (inhibitor), and the enzyme bound to Mg2+ and P-pyr (substrate). The complex with the inhibitor was obtained by cocrystallization, whereas that with the substrate was obtained by briefly soaking crystals of the ligand-free enzyme with P-pyr prior to flash cooling. The PPH structure resembles that of the other members of the PEPM/ICL superfamily and is most similar to the functionally related enzyme, PEPM. Each monomer of the dimer of dimers exhibits an (/)8 barrel fold with the eighth helix swapped between two molecules of the dimer. Both P-pyr and oxalate are anchored to the active site by Mg2+. The loop capping the active site is disordered in all three structures, in contrast to PEPM, where the equivalent loop adopts an open or disordered conformation in the unbound state but sequesters the inhibitor from solvent in the bound state. Crystal packing may have favored the open conformation of PPH even when the enzyme was cocrystallized with the oxalate inhibitor. Structure alignment of PPH with other superfamily members revealed two pairs of invariant or conservatively replaced residues that anchor the flexible gating loop. The proposed PPH catalytic mechanism is analogous to that of PEPM but includes activation of a water nucleophile with the loop Thr118 residue.