7 research outputs found

    Crystallization of a classical two-dimensional electron system: Positional and orientational orders

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    Crystallization of a classical two-dimensional one-component plasma (electrons interacting with the Coulomb repulsion in a uniform neutralizing positive background) is investigated with a molecular dynamics simulation. The positional and the orientational correlation functions are calculated for the first time. We have found an indication that the solid phase has a quasi-long-range (power-law) positional order along with a long-range orientational order. This indicates that, although the long-range Coulomb interaction is outside the scope of Mermin's theorem, the absence of ordinary crystalline order at finite temperatures applies to the electron system as well. The `hexatic' phase, which is predicted between the liquid and the solid phases by the Kosterlitz-Thouless-Halperin-Nelson-Young theory, is also discussed.Comment: 3 pages, 4 figures; Corrected typos; Double columne

    Image Registration Driven by Combined Probabilistic and Geometric Descriptors ⋆

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    Abstract. Deformable image registration in the presence of considerable contrast differences and large-scale size and shape changes represents a significant challenge for image registration. A representative driving application is the study of early brain development in neuroimaging, which requires co-registration of images of the same subject across time or building 4-D population atlases. Growth during the first few years of development involves significant changes in size and shape of anatomical structures but also rapid changes in tissue properties due to myelination and structuring that are reflected in the multi-modal Magnetic Resonance (MR) contrast measurements. We propose a new registration method that generates a mapping between brain anatomies represented as a multi-compartment model of tissue class posterior images and geometries. We transform intensity patterns into combined probabilistic and geometric descriptors that drive the matching in a diffeomorphic framework, where distances between geometries are represented using currents which does not require geometric correspondence. We show preliminary results on the registrations of neonatal brain MRIs to two-year old infant MRIs using class posteriors and surface boundaries of structures undergoing major changes. Quantitative validation demonstrates that our proposed method generates registrations that better preserve the consistency of anatomical structures over time.

    Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and assignment of disulfide bonds

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    The extremely heat-stable 5'-methylthioadenosine phosphorylase from the hyperthermophilic archaeon Pyrococcus furiosus was cloned, expressed to high levels in Escherichia coli, and purified to homogeneity by heat precipitation and affinity chromatography. The recombinant enzyme was subjected to a kinetic analysis including initial velocity and product inhibition studies. The reaction follows an ordered Bi-Bi mechanism and phosphate binding precedes nucleoside binding in the phosphorolytic direction. 5'-Methylthioadenosine phosphorylase from Pyrococcus furiosus is a hexameric protein with five cysteine residues per subunit. Analysis of the fragments obtained after digestion of the protein alkylated without previous reduction identified two intrasubunit disulfide bridges. The enzyme is very resistant to chemical denaturation and the transition midpoint for guanidinium chloride-induced unfolding was determined to be 3.0 M after 22 h incubation. This value decreases to 2.0 M in the presence of 30 mM dithiothreitol, furnishing evidence that disulfide bonds are needed for protein stability. The guanidinium chloride-induced unfolding is completely reversible as demonstrated by the analysis of the refolding process by activity assays, fluorescence measurements and SDS/PAGE. The finding of multiple disulfide bridges in 5'-methylthioadenosine phosphorylase from Pyrococcus furiosus argues strongly that disulfide bond formation may be a significant molecular strategy for stabilizing intracellular hyperthermophilic proteins

    Bioprocessing of Therapeutic Proteins from the Inclusion Bodies of Escherichia coli

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