4 resultados para Volume-fractal

em Boston University Digital Common


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http://www.archive.org/details/memorialvolumeof00andeuoft

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http://www.archive.org/details/memorialvolumeof00andeiala

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The World Wide Web (WWW or Web) is growing rapidly on the Internet. Web users want fast response time and easy access to a enormous variety of information across the world. Thus, performance is becoming a main issue in the Web. Fractals have been used to study fluctuating phenomena in many different disciplines, from the distribution of galaxies in astronomy to complex physiological control systems. The Web is also a complex, irregular, and random system. In this paper, we look at the document reference pattern at Internet Web servers and use fractal-based models to understand aspects (e.g. caching schemes) that affect the Web performance.

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We propose a new characterization of protein structure based on the natural tetrahedral geometry of the β carbon and a new geometric measure of structural similarity, called visible volume. In our model, the side-chains are replaced by an ideal tetrahedron, the orientation of which is fixed with respect to the backbone and corresponds to the preferred rotamer directions. Visible volume is a measure of the non-occluded empty space surrounding each residue position after the side-chains have been removed. It is a robust, parameter-free, locally-computed quantity that accounts for many of the spatial constraints that are of relevance to the corresponding position in the native structure. When computing visible volume, we ignore the nature of both the residue observed at each site and the ones surrounding it. We focus instead on the space that, together, these residues could occupy. By doing so, we are able to quantify a new kind of invariance beyond the apparent variations in protein families, namely, the conservation of the physical space available at structurally equivalent positions for side-chain packing. Corresponding positions in native structures are likely to be of interest in protein structure prediction, protein design, and homology modeling. Visible volume is related to the degree of exposure of a residue position and to the actual rotamers in native proteins. In this article, we discuss the properties of this new measure, namely, its robustness with respect to both crystallographic uncertainties and naturally occurring variations in atomic coordinates, and the remarkable fact that it is essentially independent of the choice of the parameters used in calculating it. We also show how visible volume can be used to align protein structures, to identify structurally equivalent positions that are conserved in a family of proteins, and to single out positions in a protein that are likely to be of biological interest. These properties qualify visible volume as a powerful tool in a variety of applications, from the detailed analysis of protein structure to homology modeling, protein structural alignment, and the definition of better scoring functions for threading purposes.