73 resultados para ARCH family

em Chinese Academy of Sciences Institutional Repositories Grid Portal


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By using AKNS [Phys. Rev. Lett. 31 (1973) 125] system and introducing the wave function, a family of interesting exact solutions of the sine-Gordon equation are constructed. These solutions seem to be some soliton, kink, and anti-kink ones respectively for the different choice of the spectrum, whereas due to the interaction between two traveling-waves they have some properties different from usual soliton, kink, and anti-kink solutions.

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The snap-through and pull-in instabilities of the micromachined arch-shaped beams under an electrostatic loading are studied both theoretically and experimentally. The pull-in instability that results in a system collision with an electrode substrate may lead to a system failure and, thus, limits the system maximum displacement. The beam/plate structure with a flat initial configuration under an electrostatic loading can only experience the pull-in instability. With the different arch configurations, the structure may experience either only the pull-in instability or the snap-through and pull-in instabilities together. As shown in our computation and experiment, those arch-shaped beams with the snap-through instability have the larger maximum displacement compared with the arch-shaped beams with only the pull-in stability and those with the flat initial configuration. The snap-through occurs by exerting a fixed load, and the structure experiences a discontinuous displacement jump without consuming power. Furthermore, after the snap-through jump, the structures are demonstrated to have the capacity to withstand further electrostatic loading without pull-in. Those properties of consuming no power and increasing the structure deflection range without pull-in is very useful in microelectromechanical systems design, which can offer better sensitivity and tuning range.

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This paper extends two-dimensional model of symmetric magnetostatic flux arches confined in stratified atmospheres (Zhang and Hu, 1992, 1993) to asymmetric models. Numerical results show that the flux structure is influenced greatly by the boundary condition of magnetic field, the force-free factor, the atmospheric pressure distribution and the position of footpoints (especially the width ratio of outlet to entrance, which differs from symmetric case).

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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.

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The molecular mechanics property is the foundation of many characters of proteins. Based on intramolecular hydrophobic force network, the representative family character underlying a protein’s mechanics property is described by a simple two-letter scheme. The tendency of a sequence to become a member of a protein family is scored according to this mathematical representation. Remote homologs of the WW-domain family could be easily designed using such a mechanistic signature of protein homology. Experimental validation showed that nearly all artificial homologs have the representative folding and bioactivity of their assigned family. Since the molecular mechanics property is the only consideration in this study, the results indicate its possible role in the generation of new members of a protein family during evolution.

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