The peptide Z-Aib-Aib-Aib-L-Ala-OtBu

The title peptide, N-benzyloxycarbonyl-alpha-aminoisobutyryl-alpha-aminoisobutyryl-alpha-aminoisobutyryl-l-alanine tert-butyl ester or Z-Aib-Aib-Aib-l-Ala-OtBu (Aib is alpha-aminoisobutyric acid, Z is benzyloxycarbonyl and OtBu indicates the tert-butyl ester), C27H42N4O7, is a left-handed helix with a right-handed conformation in the fourth residue, which is the only chiral residue. There are two 4->1 intramolecular hydrogen bonds in the structure. In the lattice, molecules are hydrogen bonded to form columns along the c axis

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

Nonpolar optical scattering of positronium in magnesium fluoride

We report the results of the analysis of the temperature broadening of the momentum distribution of delocalized Positronium (Ps) in Magnesium Fluoride in terms of optical deformation-potential scattering model (long-wavelength optical phonons). The Ps optical deformation-potential coupling constant $D_{o}$ in MgF$_{2}$ has been determined to be $(1.8\pm0.3)\times10^{9}$ eV/cm. We also show that the Ps momentum distribution is sensitive to second-order phase transitions in those crystals where optical deformation-potential scattering is allowed in one and forbidden in another crystalline phase

Radioactive heat production of six geologically important nuclides

Heat production rates for the geologically important nuclides ${}^{26}$Al, ${}^{40}$K, ${}^{60}$Fe, ${}^{232}$Th, ${}^{235}$U, and ${}^{238}$U are calculated on the basis of recent data on atomic and nuclear properties. The revised data differ by several per cent from some older values, but indicate that more recent analyses converge toward values with an accuracy sufficient for all common geoscience applications, although some possibilities for improvement still remain, especially in the case of ${}^{40}$K and with regard to the determination of half-lives. A Python script is provided for calculating heat production (https://github.com/trg818/radheat).Comment: 14 pages, 1 figur

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

BamA β16C strand and periplasmic turns are critical for outer membrane protein insertion and assembly

Outer membrane β-barrel proteins play important roles in importing nutrients, exporting wastes and conducting signals in Gram-negative bacteria, mitochondria and chloroplasts. The outer membrane proteins are inserted and assembled into the outer membrane by OMP85 family proteins. In Escherichia coli , the b-barrel assembly machinery (BAM) contains four lipoproteins BamB, BamC, BamD and BamE, and one outer membrane protein BamA, forming a "top hat"-like structure. Structural and functional studies of the E. coli BAM machinery have revealed that the rotation of periplasmic ring may trigger the barrel b1C-b6C scissor-like movement that promote the unfolded outer membrane protein insertion without using ATP. Here we report the BamA C-terminal barrel structure of Salmonella enterica Typhimurium str. LT2 and functional assays, which reveal that the BamA's C-terminal residue Trp, the b16C strand of the barrel and the periplasmic turns are critical for the functionality of BamA. These findings indicate that the unique b16C and the periplasmic turns of BamA are important for the out membrane insertion and assembly. The periplasmic turns might mediate the rotation of the periplasmic ring to the scissor-like movement of BamA b1C-b6C, triggering the outer membrane protein insertion. These results are important for understanding the outer membrane protein insertion in Gram-negative bacteria, as well as in mitochondria and chloroplasts

Ein internetbasiertes Gebäudedatenrepositorium als lebenszyklusorientierte Integrationsplattform

Der Raum dient während der Nutzung als entscheidende Referenzgröße zur Handhabung der Gebäudeinformationen. Ein raumbezogener Gebäudebeschrieb und die Verwaltung eines dynamischen Raumbuches als Daten-Repositorium stellt daher eine entscheidende Grundlage für eine effiziente Nutzung, Wartung und Modernisierung wie auch für eine fortschreibende Gebäudehistorie dar. Die Umsetzbarkeit der Konzepte wird anhand eines Prototypen validiert

Direct and indirect loading of the Ilizarov external fixator: the effect on the interfragmentary movements and compressive loads

The amount of weight bearing and the force transmission to the frame have an important influence on the results of treatment with an Ilizarov external fixator. The frame provides beneficial interfragmentary movements and compressive loads at the fracture site through elastic wires. Mobilisation can be achieved by applying a weight-bearing platform at the distal end of the fixator. The effect on the interfragmentary movements and the compressive loads in indirect and direct loading were analysed in this study using a composite tibia bone model. Displacement transducers were attached to measure the interfragmentary movements and to detect relative movements of the bone fragments and movements between the rings. The compressive loads in the osteotomy were measured with loading cells in the defect zone. The weight-bearing platform had a substantial effect on the biomechanical behaviour of the frame. It led to an indirect force transmission through the fixator with respect to the osteotomy, resulting in lower compressive loads, lower interfragmentary movements and higher mechanical stress on the frame