5,401 research outputs found

    Functional renormalization group study of the Anderson--Holstein model

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    We present a comprehensive study of the spectral and transport properties in the Anderson--Holstein model both in and out of equilibrium using the functional renormalization group (FRG). We show how the previously established machinery of Matsubara and Keldysh FRG can be extended to include the local phonon mode. Based on the analysis of spectral properties in equilibrium we identify different regimes depending on the strength of the electron--phonon interaction and the frequency of the phonon mode. We supplement these considerations with analytical results from the Kondo model. We also calculate the non-linear differential conductance through the Anderson--Holstein quantum dot and find clear signatures of the presence of the phonon mode.Comment: 19 pages, 8 figure

    Using primary instability analysis for determination of apparent liquid viscosity at jet breakup atomizing non-Newtonian Fluids

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    An internal mixing twin-fluid atomizer used for the application of cavity wax in automotive engineering is investigated. At typical pressures of 100 bars the wax material is atomized into a chamber and mixed with air at elevated pressures between 4 and 6 bars. The formed two-phase flow is further flowing along a straight tube and finally discharging through a number of radially arranged orifices undergoing a secondary atomization process. The original aim of these investigations is to provide inlet and boundary conditions for numerical simulations of the unsteady film formation on the substrate. Applying a number of optical measuring techniques, the initial secondary disintegration process, initial droplet velocities and droplet size distributions could be determined. In general, it was found that at typical distances between 10 and 20 mm between nozzle and target surface the disintegration process is not yet completely finished. Due to high initial velocities of more than 100 m/s in the spray centre, the wax material deposits to a large extent in the form of ligaments. Therefore, the measured droplet size distributions can only be taken as a rough indication for the length scales of the droplets and ligaments

    A renormalization group approach to time dependent transport through correlated quantum dots

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    We introduce a real time version of the functional renormalization group which allows to study correlation effects on nonequilibrium transport through quantum dots. Our method is equally capable to address (i) the relaxation out of a nonequilibrium initial state into a (potentially) steady state driven by a bias voltage and (ii) the dynamics governed by an explicitly time-dependent Hamiltonian. All time regimes from transient to asymptotic can be tackled; the only approximation is the consistent truncation of the flow equations at a given order. As an application we investigate the relaxation dynamics of the interacting resonant level model which describes a fermionic quantum dot dominated by charge fluctuations. Moreover, we study decoherence and relaxation phenomena within the ohmic spin-boson model by mapping the latter to the interacting resonant level model

    Mitochondrial cristae revealed with focused light.

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    Because of the diffraction resolution barrier, optical microscopes have so far failed in visualizing the mitochondrial cristae, that is, the folds of the inner membrane of this 200 to 400 nm diameter sized tubular organelle. Realizing a ∼30 nm isotropic subdiffraction resolution in isoSTED fluorescence nanoscopy, we have visualized these essential structures in the mitochondria of intact cells. We find a pronounced heterogeneity in the cristae arrangements even within individual mitochondrial tubules

    Sample preparation for STED microscopy.

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    In vivo super-resolution RESOLFT microscopy of Drosophila melanogaster

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    The oxidation status of Mic19 regulates MICOS assembly.

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    The function of mitochondria depends on the proper organization of mitochondrial membranes. The morphology of the inner membrane is regulated by the recently identified mitochondrial contact site and cristae organizing system (MICOS) complex. MICOS mutants exhibit alterations in crista formation, leading to mitochondrial dysfunction. However, the mechanisms that underlie MICOS regulation remain poorly understood. MIC19, a peripheral protein of the inner membrane and component of the MICOS complex, was previously reported to be required for the proper function of MICOS in maintaining the architecture of the inner membrane. Here, we show that human and yeast MIC19 proteins undergo oxidation in mitochondria and require the mitochondrial intermembrane space assembly (MIA) pathway, which couples the oxidation and import of mitochondrial intermembrane space proteins for mitochondrial localization. Detailed analyses identified yeast Mic19 in two different redox forms. The form that contains an intramolecular disulfide bond is bound to Mic60 of the MICOS complex. Mic19 oxidation is not essential for its integration into the MICOS complex but plays a role in MICOS assembly and the maintenance of proper inner membrane morphology. These findings suggest that Mic19 is a redox-dependent regulator of MICOS function

    Investigations by mass isotopomer analysis of the formation of D-2-hydroxyglutarate by cultured lymphoblasts from two patients with D-2-hydroxyglutaric aciduria

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    AbstractD-2-Hydroxyglutaric aciduria is an inborn error of metabolism first described in 1980. To date, more than 40 patients have been diagnosed with this disease. To identify the metabolic precursor of D-2-hydroxyglutarate (D-2-HG), cultured human lymphoblasts from two patients with D-2-HG aciduria were grown in culture medium supplemented with [U-13C6]glucose or [2H5]glutamate. Mass isotopomer distribution measurements of D-2-HG, 2-ketoglutarate (2-KG) and citrate were performed by gas chromatography-mass spectrometry. The mass isotopomer distributions in D-2-HG, 2-KG and citrate, following [U-13C6]glucose and [2H5]glutamate incubations, revealed that 2-KG interconverts rapidly to D-2-HG and that D-2-HG is formed within the mitochondria
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