1,655 research outputs found

    Cramer-Rao Lower Bound for Point Based Image Registration with Heteroscedastic Error Model for Application in Single Molecule Microscopy

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    The Cramer-Rao lower bound for the estimation of the affine transformation parameters in a multivariate heteroscedastic errors-in-variables model is derived. The model is suitable for feature-based image registration in which both sets of control points are localized with errors whose covariance matrices vary from point to point. With focus given to the registration of fluorescence microscopy images, the Cramer-Rao lower bound for the estimation of a feature's position (e.g. of a single molecule) in a registered image is also derived. In the particular case where all covariance matrices for the localization errors are scalar multiples of a common positive definite matrix (e.g. the identity matrix), as can be assumed in fluorescence microscopy, then simplified expressions for the Cramer-Rao lower bound are given. Under certain simplifying assumptions these expressions are shown to match asymptotic distributions for a previously presented set of estimators. Theoretical results are verified with simulations and experimental data

    Helium Nanodroplet Infrared Action Spectroscopy of the Proton-Bound Dimer of Hydrogen Sulfate and Formate: Examining Nuclear Quantum Effects

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    The proton-bound dimer of hydrogen sulfate and formate is an archetypal structure for ionic hydrogen-bonding complexes that contribute to biogenic aerosol nucleation. Of central importance for the structure and properties of this complex is the location of the bridging proton connecting the two conjugate base moieties. The potential energy surface for bridging proton translocation features two local minima, with the proton localized at either the formate or hydrogen sulfate moiety. However, electronic structure methods reveal a shallow potential energy surface governing proton translocation, with a barrier on the order of the zero-point energy. This shallow potential complicates structural assignment and necessitates a consideration of nuclear quantum effects. In this work, we probe the structure of this complex and its isotopologues, utilizing infrared (IR) action spectroscopy of ions captured in helium nanodroplets. The IR spectra indicate a structure in which a proton is shared between the hydrogen sulfate and formate moieties, HSO4-···H+···-OOCH. However, because of the nuclear quantum effects and vibrational anharmonicities associated with the shallow potential for proton translocation, the extent of proton displacement from the formate moiety remains unclear, requiring further experiments or more advanced theoretical treatments for additional insight

    The Detectability of Pair-Production Supernovae at z < 6

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    Nonrotating, zero metallicity stars with initial masses 140 < M < 260 solar masses are expected to end their lives as pair-production supernovae (PPSNe), in which an electron-positron pair-production instability triggers explosive nuclear burning. Interest in such stars has been rekindled by recent theoretical studies that suggest primordial molecular clouds preferentially form stars with these masses. Since metal enrichment is a local process, the resulting PPSNe could occur over a broad range of redshifts, in pockets of metal-free gas. Using the implicit hydrodynamics code KEPLER, we have calculated a set of PPSN light curves that addresses the theoretical uncertainties and allows us to assess observational strategies for finding these objects at intermediate redshifts. The peak luminosities of typical PPSNe are only slightly greater than those of Type Ia, but they remain bright much longer (~ 1 year) and have hydrogen lines. Ongoing supernova searches may soon be able to limit the contribution of these very massive stars to < 1% of the total star formation rate density out to z=2 which already provides useful constraints for theoretical models. The planned Joint Dark Energy Mission satellite will be able to extend these limits out to z=6.Comment: 12 pages, 6 figures, ApJ in press; slightly revised version, a few typos correcte

    The Chicken Yolk Sac IgY Receptor, a Mammalian Mannose Receptor Family Member, Transcytoses IgY across Polarized Epithelial Cells

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    In mammals the transfer of passive immunity from mother to young is mediated by the MHC-related receptor FcRn, which transports maternal IgG across epithelial cell barriers. In birds, maternal IgY in egg yolk is transferred across the yolk sac to passively immunize chicks during gestation and early independent life. The chicken yolk sac IgY receptor (FcRY) is the ortholog of the mammalian phospholipase A2 receptor, a mannose receptor family member, rather than an FcRn or MHC homolog. FcRn and FcRY both exhibit ligand binding at the acidic pH of endosomes and ligand release at the slightly basic pH of blood. Here we show that FcRY expressed in polarized mammalian epithelial cells functioned in endocytosis, bidirectional transcytosis, and recycling of chicken FcY/IgY. Confocal immunofluorescence studies demonstrated that IgY binding and endocytosis occurred at acidic but not basic pH, mimicking pH-dependent uptake of IgG by FcRn. Colocalization studies showed FcRY-mediated internalization via clathrin-coated pits and transport involving early and recycling endosomes. Disruption of microtubules partially inhibited apical-to-basolateral and basolateral-to-apical transcytosis, but not recycling, suggesting the use of different trafficking machinery. Our results represent the first cell biological evidence of functional equivalence between FcRY and FcRn and provide an intriguing example of how evolution can give rise to systems in which similar biological requirements in different species are satisfied utilizing distinct protein folds
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