84 resultados para Hill family.


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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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研究了空间飞行器编队中最具基础性的问题之一,即相对运动的解析表达及Hill方程的适用条件。通过建立相对运动的通解公式,针对不同性质的初值深入地分析了其相对运动轨迹的本质特征,并给出了Hill方程的适用条件。此外,文中还给出了一个新的编队设计简化公式。

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This paper presents the Hill instability analysis of Tension Leg Platform (TLP) tether it, deep sea. The 2-D nonlinear beam model which is Undergoing Coupled axial and transverse vibrations, is applied. The governing equations are reduced to nonlinear Hill equation by use of the Galerkin's method and the modes superposition principle. The Hill instability charted Lip to large parameters is obtained. An important parameter M is defined and can he expressed as the functions of tether length, the platform surge and heave motion amplitudes. Some example studies are performed for various environmental conditions. The results demonstrate that the nonlinear coupling between the axial and transverse vibrations has a significant effect on the response of structure.. It needs to be considered for the accurate dynamic analysis of long TLP tether subjected to the combined platform surge and heave motions.

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methods of lifetime measurement are discussed.

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研究了空间飞行器编队中最具基础性的问题之一,即相对运动的解析表达及Hill方程的适用条件。通过建立相对运动的通解公式,针对不同性质的初值深入地分析了其相对运动轨迹的本质特征,并给出了Hill方程的适用条件。此外,文中还给出了一个新的编队设计简化公式。

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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.