Imaging the Earth's Interior: the Angular Distribution of Terrestrial Neutrinos

Decays of radionuclides throughout the Earth's interior produce geothermal heat, but also are a source of antineutrinos. The (angle-integrated) geoneutrino flux places an integral constraint on the terrestrial radionuclide distribution. In this paper, we calculate the angular distribution of geoneutrinos, which opens a window on the differential radionuclide distribution. We develop the general formalism for the neutrino angular distribution, and we present the inverse transformation which recovers the terrestrial radioisotope distribution given a measurement of the neutrino angular distribution. Thus, geoneutrinos not only allow a means to image the Earth's interior, but offering a direct measure of the radioactive Earth, both (1) revealing the Earth's inner structure as probed by radionuclides, and (2) allowing for a complete determination of the radioactive heat generation as a function of radius. We present the geoneutrino angular distribution for the favored Earth model which has been used to calculate geoneutrino flux. In this model the neutrino generation is dominated by decays in the Earth's mantle and crust; this leads to a very ``peripheral'' angular distribution, in which 2/3 of the neutrinos come from angles > 60 degrees away from the downward vertical. We note the possibility of that the Earth's core contains potassium; different geophysical predictions lead to strongly varying, and hence distinguishable, central intensities (< 30 degrees from the downward vertical). Other uncertainties in the models, and prospects for observation of the geoneutrino angular distribution, are briefly discussed. We conclude by urging the development and construction of antineutrino experiments with angular sensitivity. (Abstract abridged.)Comment: 25 pages, RevTeX, 7 figures. Comments welcom

Outer membrane β-barrel protein folding is physically controlled by periplasmic lipid head groups and BamA.

Outer membrane β-barrel proteins (OMPs) are crucial for numerous cellular processes in prokaryotes and eukaryotes. Despite extensive studies on OMP biogenesis, it is unclear why OMPs require assembly machineries to fold into their native outer membranes, as they are capable of folding quickly and efficiently through an intrinsic folding pathway in vitro. By investigating the folding of several bacterial OMPs using membranes with naturally occurring Escherichia coli lipids, we show that phosphoethanolamine and phosphoglycerol head groups impose a kinetic barrier to OMP folding. The kinetic retardation of OMP folding places a strong negative pressure against spontaneous incorporation of OMPs into inner bacterial membranes, which would dissipate the proton motive force and undoubtedly kill bacteria. We further show that prefolded β-barrel assembly machinery subunit A (BamA), the evolutionarily conserved, central subunit of the BAM complex, accelerates OMP folding by lowering the kinetic barrier imposed by phosphoethanolamine head groups. Our results suggest that OMP assembly machineries are required in vivo to enable physical control over the spontaneously occurring OMP folding reaction in the periplasm. Mechanistic studies further allowed us to derive a model for BamA function, which explains how OMP assembly can be conserved between prokaryotes and eukaryotes.This is the author accepted manuscript. The final version is available from the National Academy of Sciences via http://dx.doi.org/10.1073/pnas.132247311

The Borrelia afzelii outer membrane protein BAPKO_0422 binds human Factor-H and is predicted to form a membrane-spanning beta-barrel

The deep evolutionary history of the Spirochetes places their branch point early in the evolution of the diderms, before the divergence of the present day Proteobacteria. As a Spirochete, the morphology of the Borrelia cell envelope shares characteristics of both Gram-positive and Gram-negative bacteria. A thin layer of peptidoglycan, tightly associated with the cytoplasmic membrane is surrounded by a more labile outer membrane (OM). This OM is rich in lipoproteins but with few known integral membrane proteins. The OmpA domain is an eight-stranded membrane-spanning β-barrel, highly conserved among the Proteobacteria but so far unknown in the Spirochetes. In the present work we describe the identification of four novel OmpA-like β-barrels from Borrelia afzelii, the most common cause of erythema migrans rash in Europe. Structural characterisation of one these proteins (BAPKO_0422) by small angle X-ray scattering (SAXS) and circular dichroism indicate a compact globular structure rich in β-strand consistent with a monomeric β-barrel. Ab initio molecular envelopes calculated from the scattering profile are consistent with homology models and demonstrate that BAPKO_0422 adopts a peanut shape with dimensions 25 x 45 Å. Deviations from the standard C-terminal signature sequence are apparent; in particular the C-terminal Phe residue commonly found in Proteobacterial OM proteins is replaced by Ile/Leu or Asn. BAPKO_0422 is demonstrated to bind human factor-H and therefore may contribute to immune evasion by inhibition of the complement response. Encoded by chromosomal genes, these proteins are highly conserved between Borrelia subspecies and may be of diagnostic or therapeutic value

Molecular Modeling of Mechanosensory Ion Channel Structural and Functional Features

The DEG/ENaC (Degenerin/Epithelial Sodium Channel) protein family comprises related ion channel subunits from all metazoans, including humans. Members of this protein family play roles in several important biological processes such as transduction of mechanical stimuli, sodium re-absorption and blood pressure regulation. Several blocks of amino acid sequence are conserved in DEG/ENaC proteins, but structure/function relations in this channel class are poorly understood. Given the considerable experimental limitations associated with the crystallization of integral membrane proteins, knowledge-based modeling is often the only route towards obtaining reliable structural information. To gain insight into the structural characteristics of DEG/ENaC ion channels, we derived three-dimensional models of MEC-4 and UNC-8, based on the available crystal structures of ASIC1 (Acid Sensing Ion Channel 1). MEC-4 and UNC-8 are two DEG/ENaC family members involved in mechanosensation and proprioception respectively, in the nematode Caenorhabditis elegans. We used these models to examine the structural effects of specific mutations that alter channel function in vivo. The trimeric MEC-4 model provides insight into the mechanism by which gain-of-function mutations cause structural alterations that result in increased channel permeability, which trigger cell degeneration. Our analysis provides an introductory framework to further investigate the multimeric organization of the DEG/ENaC ion channel complex

Structural basis of outer membrane protein insertion by the BAM complex

All Gram-negative bacteria, mitochondria and chloroplasts have outer membrane proteins (OMPs) that perform many fundamental biological processes. The OMPs in Gram-negative bacteria are inserted and folded into the outer membrane by the β-barrel assembly machinery (BAM). The mechanism involved is poorly understood, owing to the absence of a structure of the entire BAM complex. Here we report two crystal structures of the Escherichia coli BAM complex in two distinct states: an inward-open state and a lateral-open state. Our structures reveal that the five polypeptide transport-associated domains of BamA form a ring architecture with four associated lipoproteins, BamB–BamE, in the periplasm. Our structural, functional studies and molecular dynamics simulations indicate that these subunits rotate with respect to the integral membrane β-barrel of BamA to induce movement of the β-strands of the barrel and promote insertion of the nascent OMP

Mass dependent fractionation of stable chromium isotopes in mare basalts: implications for the formation and differentiation of the Moon

We present the first stable chromium isotopic data from mare basalts in order to investigate the similarity between the Moon and the Earth’s mantle. A double spike technique coupled with MC-ICP-MS measurements was used to analyse 19 mare basalts, comprising high-Ti, low-Ti and KREEP-rich varieties. Chromium isotope ratios (δ53Cr) for mare basalts are positively correlated with indices of magmatic differentiation such as Mg# and Cr concentration which suggests that Cr isotopes were fractionated during magmatic differentiation. Modelling of the results provides evidence that spinel and pyroxene are the main phases controlling the Cr isotopic composition during fractional crystallisation. The most evolved samples have the lightest isotopic compositions, complemented by cumulates that are isotopically heavy. Two hypotheses are proposed to explain this fractionation: (i) equilibrium fractionation where heavy isotopes are preferentially incorporated into the spinel lattice and (ii) a difference in isotopic composition between Cr2+ and Cr3+ in the melt. However, both processes require magmatic temperatures below 1200 °C for appreciable Cr3+ to be present at the low oxygen fugacities found in the Moon (IW −1 to −2 log units). There is no isotopic difference between the most primitive high-Ti, low-Ti and KREEP basalts, which suggest that the sources of these basalts were homogeneous in terms of stable Cr isotopes. The least differentiated sample in our sample set is the low-Ti basalt 12016, characterised by a Cr isotopic composition of −0.222 ± 0.025‰, which is within error of the current BSE value (−0.124 ± 0.101‰). The similarity between the mantles of the Moon and Earth is consistent with a terrestrial origin for a major fraction of the lunar Cr. This similarity also suggests that Cr isotopes were not fractionated by core formation on the Moon

Outer membrane protein folding from an energy landscape perspective

The cell envelope is essential for the survival of Gram-negative bacteria. This specialised membrane is densely packed with outer membrane proteins (OMPs), which perform a variety of functions. How OMPs fold into this crowded environment remains an open question. Here, we review current knowledge about OFMP folding mechanisms in vitro and discuss how the need to fold to a stable native state has shaped their folding energy landscapes. We also highlight the role of chaperones and the β-barrel assembly machinery (BAM) in assisting OMP folding in vivo and discuss proposed mechanisms by which this fascinating machinery may catalyse OMP folding

Effects of Periplasmic Chaperones and Membrane Thickness on BamA-Catalyzed Outer-Membrane Protein Folding

The biogenesis of outer-membrane proteins (OMPs) in gram-negative bacteria involves delivery by periplasmic chaperones to the β-barrel assembly machinery (BAM), which catalyzes OMP insertion into the outer membrane. Here, we examine the effects of membrane thickness, the Escherichia coli periplasmic chaperones Skp and SurA, and BamA, the central subunit of the BAM complex, on the folding kinetics of a model OMP (tOmpA) using fluorescence spectroscopy, native mass spectrometry, and molecular dynamics simulations. We show that prefolded BamA promotes the release of tOmpA from Skp despite the nM affinity of the Skp:tOmpA complex. This activity is located in the BamA β-barrel domain, but is greater when full-length BamA is present, indicating that both the β-barrel and polypeptide transport-associated (POTRA) domains are required for maximal activity. By contrast, SurA is unable to release tOmpA from Skp, providing direct evidence against a sequential chaperone model. By varying lipid acyl chain length in synthetic liposomes we show that BamA has a greater catalytic effect on tOmpA folding in thicker bilayers, suggesting that BAM catalysis involves lowering of the kinetic barrier imposed by the hydrophobic thickness of the membrane. Consistent with this, molecular dynamics simulations reveal that increases in membrane thinning/disorder by the transmembrane domain of BamA is greatest in thicker bilayers. Finally, we demonstrate that cross-linking of the BamA barrel does not affect tOmpA folding kinetics in 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) liposomes, suggesting that lateral gating of the BamA barrel and/or hybrid barrel formation is not required, at least for the assembly of a small 8-stranded OMP in vitro

Experimental study of platinum solubility in silicate melt to 14 GPa and 2273 K: Implications for accretion and core formation in Earth

We determined the solubility limit of Pt in molten haplo-basalt (1 atm anorthite-diopside eutectic composition) in piston-cylinder and multi-anvil experiments at pressures between 0.5 and 14 GPa and temperatures from 1698 to 2223 K. Experiments were internally buffered at ∼IW + 1. Pt concentrations in quenched-glass samples were measured by laser-ablation inductively coupled-plasma mass spectrometry (LA-ICPMS). This technique allows detection of small-scale heterogeneities in the run products while supplying three-dimensional information about the distribution of Pt in the glass samples. Analytical variations in 195Pt indicate that all experiments contain Pt nanonuggets after quenching. Averages of multiple, time-integrated spot analyses (corresponding to bulk analyses) typically have large standard deviations, and calculated Pt solubilities in silicate melt exhibit no statistically significant covariance with temperature or pressure. In contrast, averages of minimum 195Pt signal levels show less inter-spot variation, and solubility shows significant covariance with pressure and temperature. We interpret these results to mean that nanonuggets are not quench particles, that is, they were not dissolved in the silicate melt, but were part of the equilibrium metal assemblage at run conditions. We assume that the average of minimum measured Pt abundances in multiple probe spots is representative of the actual solubility. The metal/silicate partition coefficients (Dmet/sil) is the inverse of solubility, and we parameterize Dmet/sil in the data set by multivariate regression. The statistically robust regression shows that increasing both pressure and temperature causes Dmet/silto decrease, that is, Pt becomes more soluble in silicate melt. Dmet/sil decreases by less than an order of magnitude at constant temperature from 1 to 14 GPa, whereas isobaric increase in temperature produces a more dramatic effect, with Dmet/sil decreasing by more than one order of magnitude between 1623 and 2223 K. The Pt abundance in the Earth’s mantle requires that Dmet/sil is ∼1000 assuming core-mantle equilibration. Geochemical models for core formation in Earth based on moderately and slightly siderophile elements are generally consistent with equilibrium metal segregation at conditions generally in the range of 20–60 GPa and 2000–4000 K. Model extrapolations to these conditions show that the Pt abundance of the mantle can only be matched if oxygen fugacity is high (∼IW) and if Pt mixes ideally in molten iron, both very unlikely conditions. For more realistic values of oxygen fugacity (∼IW − 2) and experimentally-based constraints on non-ideal mixing, models show that Dmet/sil would be several orders of magnitude too high even at the most favorable conditions of pressure and temperature. These results suggest that the mantle Pt budget, and by implication other highly siderophile elements, was added by late addition of a ‘late veneer’ phase to the accreting proto-Earth