1000 resultados para BAND ALIGNMENT


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Time variability of the scattering signals from wind turbines may lead to degradation problems on the communication systems provided in the UHF band, especially under near field condition. In order to analyze the variability due to the rotation of the blades, this paper characterizes empirical Doppler spectra obtained from real samples of signals scattered by wind turbines with rotating blades under near field condition. A new Doppler spectrum model is proposed to fit the spectral characteristics of these signals, providing notable goodness of fit. Finally, the effect of this kind of time variability on the degradation of OFDM signals is studied.

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Santamaría, José Miguel; Pajares, Eterio; Olsen, Vickie; Merino, Raquel; Eguíluz, Federico (eds.)

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We derive an explicit expression for predicting the thicknesses of shear bands in metallic glasses. The model demonstrates that the shear-band thickness is mainly dominated by the activation size of the shear transformation zone (STZ) and its activation free volume concentration. The predicted thicknesses agree well with the results of measurements and simulations. The underlying physics is attributed to the local topological instability of the activated STZ. The result is of significance in understanding the origin of inhomogeneous flow in metallic glasses. (C) 2009 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.

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As a basic tool of modern biology, sequence alignment can provide us useful information in fold, function, and active site of protein. For many cases, the increased quality of sequence alignment means a better performance. The motivation of present work is to increase ability of the existing scoring scheme/algorithm by considering residue–residue correlations better. Based on a coarse-grained approach, the hydrophobic force between each pair of residues is written out from protein sequence. It results in the construction of an intramolecular hydrophobic force network that describes the whole residue–residue interactions of each protein molecule, and characterizes protein's biological properties in the hydrophobic aspect. A former work has suggested that such network can characterize the top weighted feature regarding hydrophobicity. Moreover, for each homologous protein of a family, the corresponding network shares some common and representative family characters that eventually govern the conservation of biological properties during protein evolution. In present work, we score such family representative characters of a protein by the deviation of its intramolecular hydrophobic force network from that of background. Such score can assist the existing scoring schemes/algorithms, and boost up the ability of multiple sequences alignment, e.g. achieving a prominent increase (50%) in searching the structurally alike residue segments at a low identity level. As the theoretical basis is different, the present scheme can assist most existing algorithms, and improve their efficiency remarkably.