2 resultados para Dihydrolipoyllysine-Residue Acetyltransferase

em Boston University Digital Common


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In gesture and sign language video sequences, hand motion tends to be rapid, and hands frequently appear in front of each other or in front of the face. Thus, hand location is often ambiguous, and naive color-based hand tracking is insufficient. To improve tracking accuracy, some methods employ a prediction-update framework, but such methods require careful initialization of model parameters, and tend to drift and lose track in extended sequences. In this paper, a temporal filtering framework for hand tracking is proposed that can initialize and reset itself without human intervention. In each frame, simple features like color and motion residue are exploited to identify multiple candidate hand locations. The temporal filter then uses the Viterbi algorithm to select among the candidates from frame to frame. The resulting tracking system can automatically identify video trajectories of unambiguous hand motion, and detect frames where tracking becomes ambiguous because of occlusions or overlaps. Experiments on video sequences of several hundred frames in duration demonstrate the system's ability to track hands robustly, to detect and handle tracking ambiguities, and to extract the trajectories of unambiguous hand motion.

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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.