22 resultados para Ceremonial entries


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The maximal rate of a nonsquare complex orthogonal design for transmit antennas is 1/2 + 1/n if is even and 1/2 + 1/n+1 if is odd and the codes have been constructed for all by Liang (2003) and Lu et al. (2005) to achieve this rate. A lower bound on the decoding delay of maximal-rate complex orthogonal designs has been obtained by Adams et al. (2007) and it is observed that Liang's construction achieves the bound on delay for equal to 1 and 3 modulo 4 while Lu et al.'s construction achieves the bound for n = 0, 1, 3 mod 4. For n = 2 mod 4, Adams et al. (2010) have shown that the minimal decoding delay is twice the lower bound, in which case, both Liang's and Lu et al.'s construction achieve the minimum decoding delay. For large value of, it is observed that the rate is close to half and the decoding delay is very large. A class of rate-1/2 codes with low decoding delay for all has been constructed by Tarokh et al. (1999). In this paper, another class of rate-1/2 codes is constructed for all in which case the decoding delay is half the decoding delay of the rate-1/2 codes given by Tarokh et al. This is achieved by giving first a general construction of square real orthogonal designs which includes as special cases the well-known constructions of Adams, Lax, and Phillips and the construction of Geramita and Pullman, and then making use of it to obtain the desired rate-1/2 codes. For the case of nine transmit antennas, the proposed rate-1/2 code is shown to be of minimal delay. The proposed construction results in designs with zero entries which may have high peak-to-average power ratio and it is shown that by appropriate postmultiplication, a design with no zero entry can be obtained with no change in the code parameters.

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Purpose: To optimize the data-collection strategy for diffuse optical tomography and to obtain a set of independent measurements among the total measurements using the model based data-resolution matrix characteristics. Methods: The data-resolution matrix is computed based on the sensitivity matrix and the regularization scheme used in the reconstruction procedure by matching the predicted data with the actual one. The diagonal values of data-resolution matrix show the importance of a particular measurement and the magnitude of off-diagonal entries shows the dependence among measurements. Based on the closeness of diagonal value magnitude to off-diagonal entries, the independent measurements choice is made. The reconstruction results obtained using all measurements were compared to the ones obtained using only independent measurements in both numerical and experimental phantom cases. The traditional singular value analysis was also performed to compare the results obtained using the proposed method. Results: The results indicate that choosing only independent measurements based on data-resolution matrix characteristics for the image reconstruction does not compromise the reconstructed image quality significantly, in turn reduces the data-collection time associated with the procedure. When the same number of measurements (equivalent to independent ones) are chosen at random, the reconstruction results were having poor quality with major boundary artifacts. The number of independent measurements obtained using data-resolution matrix analysis is much higher compared to that obtained using the singular value analysis. Conclusions: The data-resolution matrix analysis is able to provide the high level of optimization needed for effective data-collection in diffuse optical imaging. The analysis itself is independent of noise characteristics in the data, resulting in an universal framework to characterize and optimize a given data-collection strategy. (C) 2012 American Association of Physicists in Medicine. http://dx.doi.org/10.1118/1.4736820]

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We show that as n changes, the characteristic polynomial of the n x n random matrix with i.i.d. complex Gaussian entries can be described recursively through a process analogous to Polya's urn scheme. As a result, we get a random analytic function in the limit, which is given by a mixture of Gaussian analytic functions. This suggests another reason why the zeros of Gaussian analytic functions and the Ginibre ensemble exhibit similar local repulsion, but different global behavior. Our approach gives new explicit formulas for the limiting analytic function.

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In this work, we address the recovery of block sparse vectors with intra-block correlation, i.e., the recovery of vectors in which the correlated nonzero entries are constrained to lie in a few clusters, from noisy underdetermined linear measurements. Among Bayesian sparse recovery techniques, the cluster Sparse Bayesian Learning (SBL) is an efficient tool for block-sparse vector recovery, with intra-block correlation. However, this technique uses a heuristic method to estimate the intra-block correlation. In this paper, we propose the Nested SBL (NSBL) algorithm, which we derive using a novel Bayesian formulation that facilitates the use of the monotonically convergent nested Expectation Maximization (EM) and a Kalman filtering based learning framework. Unlike the cluster-SBL algorithm, this formulation leads to closed-form EMupdates for estimating the correlation coefficient. We demonstrate the efficacy of the proposed NSBL algorithm using Monte Carlo simulations.

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An online computing server, Online_DPI (where DPI denotes the diffraction precision index), has been created to calculate the `Cruickshank DPI' value for a given three-dimensional protein or macromolecular structure. It also estimates the atomic coordinate error for all the atoms available in the structure. It is an easy-to-use web server that enables users to visualize the computed values dynamically on the client machine. Users can provide the Protein Data Bank (PDB) identification code or upload the three-dimensional atomic coordinates from the client machine. The computed DPI value for the structure and the atomic coordinate errors for all the atoms are included in the revised PDB file. Further, users can graphically view the atomic coordinate error along with `temperature factors' (i.e. atomic displacement parameters). In addition, the computing engine is interfaced with an up-to-date local copy of the Protein Data Bank. New entries are updated every week, and thus users can access all the structures available in the Protein Data Bank. The computing engine is freely accessible online at http://cluster.physics.iisc.ernet.in/dpi/.

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The power of X-ray crystal structure analysis as a technique is to `see where the atoms are'. The results are extensively used by a wide variety of research communities. However, this `seeing where the atoms are' can give a false sense of security unless the precision of the placement of the atoms has been taken into account. Indeed, the presentation of bond distances and angles to a false precision (i.e. to too many decimal places) is commonplace. This article has three themes. Firstly, a basis for a proper representation of protein crystal structure results is detailed and demonstrated with respect to analyses of Protein Data Bank entries. The basis for establishing the precision of placement of each atom in a protein crystal structure is non-trivial. Secondly, a knowledge base harnessing such a descriptor of precision is presented. It is applied here to the case of salt bridges, i.e. ion pairs, in protein structures; this is the most fundamental place to start with such structure-precision representations since salt bridges are one of the tenets of protein structure stability. Ion pairs also play a central role in protein oligomerization, molecular recognition of ligands and substrates, allosteric regulation, domain motion and alpha-helix capping. A new knowledge base, SBPS (Salt Bridges in Protein Structures), takes these structural precisions into account and is the first of its kind. The third theme of the article is to indicate natural extensions of the need for such a description of precision, such as those involving metalloproteins and the determination of the protonation states of ionizable amino acids. Overall, it is also noted that this work and these examples are also relevant to protein three-dimensional structure molecular graphics software.

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We show that the density of eigenvalues for three classes of random matrix ensembles is determinantal. First we derive the density of eigenvalues of product of k independent n x n matrices with i.i.d. complex Gaussian entries with a few of matrices being inverted. In second example we calculate the same for (compatible) product of rectangular matrices with i.i.d. Gaussian entries and in last example we calculate for product of independent truncated unitary random matrices. We derive exact expressions for limiting expected empirical spectral distributions of above mentioned ensembles.