A family of interesting exact solutions of the sine-Gordon equation

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.

A hall dynamo model for the reversed field pinch

A mechanism for the reversed field pinch (RFP) dynamo is proposed, based on the nonlinear Hall effect of a saturated helical MHD instability. The sign and magnitude of the effect are shown to be those required for the RFP dynamo. Predictions of the model are in accord with RFP fluctuation measurements.

SiC_p/6151Al复合材料的微结构效应

利用分离式Hopkinson压杆和MTS通用材料试验机研究了SiC_p/6151Al颗粒增强复合材料在不同应变率下的变形行为和增强颗粒的尺寸对复合材料微结构及变形行为的影响。结果表明，对于在不同应变率下的SiC_p/6151Al复合材料，增强颗粒尺寸大小的流动应力高于增强颗粒尺寸的流动应力。根据位错强化理论中的Hall-Petch关系对这个结果进行了解释。首次在实验上观测到增强颗粒对复合材料微损伤-微带形成的影响，并根据微带（microband）形成的双位错墙理论（double dislocation walls）, 分析了增强颗粒对复合材料微带损伤及力学性能影响的微结构效应。

A scheme for multiple sequences alignment optimization-an improvement based on family representative mechanics features

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.

Generating artificial homologous proteins according to the representative family character in molecular mechanics properties - an attempt in validating an underlying rule of protein evolution

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.