3 resultados para Ossat, Arnaud de (1536-1604)

em Boston University Digital Common


Relevância:

10.00% 10.00%

Publicador:

Resumo:

University of California Libraries

Relevância:

10.00% 10.00%

Publicador:

Resumo:

Anomalies are unusual and significant changes in a network's traffic levels, which can often involve multiple links. Diagnosing anomalies is critical for both network operators and end users. It is a difficult problem because one must extract and interpret anomalous patterns from large amounts of high-dimensional, noisy data. In this paper we propose a general method to diagnose anomalies. This method is based on a separation of the high-dimensional space occupied by a set of network traffic measurements into disjoint subspaces corresponding to normal and anomalous network conditions. We show that this separation can be performed effectively using Principal Component Analysis. Using only simple traffic measurements from links, we study volume anomalies and show that the method can: (1) accurately detect when a volume anomaly is occurring; (2) correctly identify the underlying origin-destination (OD) flow which is the source of the anomaly; and (3) accurately estimate the amount of traffic involved in the anomalous OD flow. We evaluate the method's ability to diagnose (i.e., detect, identify, and quantify) both existing and synthetically injected volume anomalies in real traffic from two backbone networks. Our method consistently diagnoses the largest volume anomalies, and does so with a very low false alarm rate.

Relevância:

10.00% 10.00%

Publicador:

Resumo:

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.