999 resultados para Library architecture.


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REDEFINE is a reconfigurable SoC architecture that provides a unique platform for high performance and low power computing by exploiting the synergistic interaction between coarse grain dynamic dataflow model of computation (to expose abundant parallelism in applications) and runtime composition of efficient compute structures (on the reconfigurable computation resources). We propose and study the throttling of execution in REDEFINE to maximize the architecture efficiency. A feature specific fast hybrid (mixed level) simulation framework for early in design phase study is developed and implemented to make the huge design space exploration practical. We do performance modeling in terms of selection of important performance criteria, ranking of the explored throttling schemes and investigate effectiveness of the design space exploration using statistical hypothesis testing. We find throttling schemes which give appreciable (24.8%) overall performance gain in the architecture and 37% resource usage gain in the throttling unit simultaneously.

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Ten new cyclic hexadepsipeptides, six isariins and four isaridins, from the fungus Isaria have been identified and characterized by high-performance liquid chromatography, coupled to tandem electrospray ionization mass spectrometry (LC-ESIMS/MS). The isariins possess a beta-hydroxy acid residue and five alpha-amino acids, while isaridins contain a beta-amino acid, an alpha-hydroxy acid, and four alpha-amino acids. One- and two-dimensional NMR spectroscopy confirmed the chemical identity of some of the isariin fractions. Mass spectral fragmentation patterns of [M + H](+) ions reveal clear diagnostic fragment ions for the isariins and isaridins. Previously described cyclic depsipeptides, isarfelins from Isaria felina (Guo, Y. X.; Liu, Q. H.; Ng, T. B.; Wang H. X. Peptides 2005, 26, 2384), are now reassigned as members of the isaridin family. Examination of isaridin sequences revealed significant similarities with cyclic hexadepsipeptides such as destruxins and roseotoxins. The structure of an isariin (isariin A) investigated by NMR spectroscopy indicated the presence of a hybrid alpha beta C-11 turn, formed by the beta-hydroxy acid and glycine residues and a (D)Leu-(L)Ala type II' beta-turn. Additionally, the inhibitory effect of isariins and an isaridin on the intra-erythrocytic growth of Plasmodium falciparum is presented.