Seven years among the Freedmen [electronic resource] / M. Waterbury

http://www.archive.org/details/sevenyearsamong00waterich/

The day-breaking, if not the sun-rising of the Gospell with the Indians in New-England.

University of California Libraries

Explaining World Wide Web Traffic Self-Similarity

Recently the notion of self-similarity has been shown to apply to wide-area and local-area network traffic. In this paper we examine the mechanisms that give rise to self-similar network traffic. We present an explanation for traffic self-similarity by using a particular subset of wide area traffic: traffic due to the World Wide Web (WWW). Using an extensive set of traces of actual user executions of NCSA Mosaic, reflecting over half a million requests for WWW documents, we show evidence that WWW traffic is self-similar. Then we show that the self-similarity in such traffic can be explained based on the underlying distributions of WWW document sizes, the effects of caching and user preference in file transfer, the effect of user "think time", and the superimposition of many such transfers in a local area network. To do this we rely on empirically measured distributions both from our traces and from data independently collected at over thirty WWW sites.

Visible Volume: a Robust Measure for Protein Structure Characterization

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.