306 research outputs found

    Local optical field variation in the neighborhood of a semiconductor micrograting

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    The local optical field of a semiconductor micrograting (GaAs, 10x10 micro m) is recorded in the middle field region using an optical scanning probe in collection mode at constant height. The recorded image shows the micro-grating with high contrast and a displaced diffraction image. The finite penetration depth of the light leads to a reduced edge resolution in the direction to the illuminating beam direction while the edge contrast in perpendicular direction remains high (~100nm). We use the discrete dipole model to calculate the local optical field to show how the displacement of the diffraction image increases with increasing distance from the surface.Comment: 12 pages, 3 figure

    Cytoplasmic anchorage of L-selectin controls leukocyte capture and rolling by increasing the mechanical stability of the selectin tether

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    L-selectin is a leukocyte lectin that mediates leukocyte capture and rolling in the vasculature. The cytoplasmic domain of L-selectin has been shown to regulate leukocyte rolling. In this study, the regulatory mechanisms by which this domain controls L-selectin adhesiveness were investigated. We report that an L-selectin mutant generated by truncation of the COOH-terminal 11 residues of L-selectin tail, which impairs association with the cytoskeletal protein α-actinin, could capture leukocytes to glycoprotein L-selectin ligands under physiological shear flow. However, the conversion of initial tethers into rolling was impaired by this partial tail truncation, and was completely abolished by a further four-residue truncation of the L-selectin tail. Physical anchorage of both cell-free tail-truncated mutants within a substrate fully rescued their adhesive deficiencies. Microkinetic analysis of full-length and truncated L-selectin–mediated rolling at millisecond temporal resolution suggests that the lifetime of unstressed L-selectin tethers is unaffected by cytoplasmic tail truncation. However, cytoskeletal anchorage of L-selectin stabilizes the selectin tether by reducing the sensitivity of its dissociation rate to increasing shear forces. Low force sensitivity (reactive compliance) of tether lifetime is crucial for selectins to mediate leukocyte rolling under physiological shear stresses. This is the first demonstration that reduced reactive compliance of L-selectin tethers is regulated by cytoskeletal anchorage, in addition to intrinsic mechanical properties of the selectin–carbohydrate bond

    Luttinger liquid behavior in weakly disordered quantum wires

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    We have measured the temperature dependence of the conductance in long V-groove quantum wires (QWRs) fabricated in GaAs/AlGaAs heterostructures. Our data is consistent with recent theories developed within the framework of the Luttinger liquid model, in the limit of weakly disordered wires. We show that for the relatively small amount of disorder in our QWRs, the value of the interaction parameter g is g=0.66, which is the expected value for GaAs. However, samples with a higher level of disorder show conductance with stronger temperature dependence, which does not allow their treatment in the framework of perturbation theory. Trying to fit such data with perturbation-theory models leads inevitably to wrong (lower) values of g.Comment: 4 pages, 4 figure

    Synthesis of novel poly(dG)-poly(dG)-poly(dC) triplex structure by Klenow exo− fragment of DNA polymerase I

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    The extension of the G-strand of long (700 bp) poly(dG)-poly(dC) by the Klenow exo− fragment of DNA polymerase I yields a complete triplex structure of the H-DNA type. High-performance liquid chromatography analysis demonstrates that the length of the G-strand is doubled during the polymerase synthesis. Fluorescence resonance energy transfer analysis shows that the 5′ ends of the G- and the C-strands, labeled with fluorescein and TAMRA, respectively, are positioned close to each other in the product of the synthesis. Atomic force microscopy morphology imaging shows that the synthesized structures lack single-stranded fragments and have approximately the same length as the parent 700 bp poly(dG)-poly(dC). CD spectrum of the polymer has a large negative peak at 278 nm, which is characteristic of the poly(dG)-poly(dG)-poly(dC) triplex. The polymer is resistant to DNase and interacts much more weakly with ethidium bromide as compared with the double-stranded DN

    Synthesis of novel poly(dG)–poly(dG)–poly(dC) triplex structure by Klenow exo(−) fragment of DNA polymerase I

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    The extension of the G-strand of long (700 bp) poly(dG)–poly(dC) by the Klenow exo(−) fragment of DNA polymerase I yields a complete triplex structure of the H-DNA type. High-performance liquid chromatography analysis demonstrates that the length of the G-strand is doubled during the polymerase synthesis. Fluorescence resonance energy transfer analysis shows that the 5′ ends of the G- and the C-strands, labeled with fluorescein and TAMRA, respectively, are positioned close to each other in the product of the synthesis. Atomic force microscopy morphology imaging shows that the synthesized structures lack single-stranded fragments and have approximately the same length as the parent 700 bp poly(dG)–poly(dC). CD spectrum of the polymer has a large negative peak at 278 nm, which is characteristic of the poly(dG)–poly(dG)–poly(dC) triplex. The polymer is resistant to DNase and interacts much more weakly with ethidium bromide as compared with the double-stranded DNA

    Enhancement of the Binding Energy of Charged Excitons in Disordered Quantum Wires

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    Negatively and positively charged excitons are identified in the spatially-resolved photoluminescence spectra of quantum wires. We demonstrate that charged excitons are weakly localized in disordered quantum wires. As a consequence, the enhancement of the "binding energy" of a charged exciton is caused, for a significant part, by the recoil energy transferred to the remaining charged carrier during its radiative recombination. We discover that the Coulomb correlation energy is not the sole origin of the "binding energy", in contrast to charged excitons confined in quantum dots.Comment: 4 Fig

    Stability of adhesion clusters under constant force

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    We solve the stochastic equations for a cluster of parallel bonds with shared constant loading, rebinding and the completely dissociated state as an absorbing boundary. In the small force regime, cluster lifetime grows only logarithmically with bond number for weak rebinding, but exponentially for strong rebinding. Therefore rebinding is essential to ensure physiological lifetimes. The number of bonds decays exponentially with time for most cases, but in the intermediate force regime, a small increase in loading can lead to much faster decay. This effect might be used by cell-matrix adhesions to induce signaling events through cytoskeletal loading.Comment: Revtex, 4 pages, 4 Postscript files include

    Avidity enhancement of L-selectin bonds by flow: shear-promoted rotation of leukocytes turn labile bonds into functional tethers

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    L-selectin is a key lectin essential for leukocyte capture and rolling on vessel walls. Functional adhesion of L-selectin requires a minimal threshold of hydrodynamic shear. Using high temporal resolution videomicroscopy, we now report that L-selectin engages its ligands through exceptionally labile adhesive bonds (tethers) even below this shear threshold. These tethers share a lifetime of 4 ms on distinct physiological ligands, two orders of magnitude shorter than the lifetime of the P-selectin–PSGL-1 bond. Below threshold shear, tether duration is not shortened by elevated shear stresses. However, above the shear threshold, selectin tethers undergo 14-fold stabilization by shear-driven leukocyte transport. Notably, the cytoplasmic tail of L-selectin contributes to this stabilization only above the shear threshold. These properties are not shared by P-selectin– or VLA-4–mediated tethers. L-selectin tethers appear adapted to undergo rapid avidity enhancement by cellular transport, a specialized mechanism not used by any other known adhesion receptor
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