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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Catalysis letters 40 (1996), S. 115-118 
    ISSN: 1572-879X
    Keywords: carbon dioxide hydrogenation ; iron-potassium catalyst ; hydrocarbons
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The hydrogenation of CO2 has been studied over Fe/alumina and Fe-K/alumina catalysts. The addition of potassium increases the chemisorption ability of CO2 but decreases that of H2. The catalytic activity test at high pressure (20 atm) reveals that remarkably high activity and selectivity toward light olefins and C2+ hydrocarbons can be achieved with Fe-K/alumina catalysts containing high concentration of K (K/Fe molar ratio = 0.5, 1.0). In the reaction at atmospheric pressure, the highly K-promoted catalysts give much higher CO formation rate than the unpromoted catalyst. It is deduced that the remarkable catalytic properties in the presence of K are attributable to the increase in the ability of CO2 chemisorption and the enhanced activity for CO formation, which is the preceding step of C2+ hydrocarbon formation.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature structural & molecular biology 11 (2004), S. 365-370 
    ISSN: 1545-9985
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] SCFFbs1 is a ubiquitin ligase that functions in the endoplasmic reticulum (ER)-associated degradation pathway. Fbs1/Fbx2, a member of the F-box proteins, recognizes high-mannose oligosaccharides. Efficient binding to an N-glycan requires di-N-acetylchitobiose (chitobiose). Here we report the ...
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    [s.l.] : Macmillian Magazines Ltd.
    Nature 435 (2005), S. 693-696 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Nuclear protein import is mediated mainly by the transport factor importin-β that binds cytoplasmic cargo, most often via the importin-α adaptor, and then transports it through nuclear pore complexes. This active transport is driven by disassembly of the import complex by nuclear ...
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 941-947 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The X-ray structure of bovine heart cytochrome c oxidase solved for orthorhombic crystals showed a dimeric structure stabilized by four subunit–subunit contacts, namely, subunit Vb–subunit Vb on the matrix side, subunit I–subunit VIa, subunit VIa–subunit I in the transmembrane region and subunit VIb–subunit VIb on the intermembrane side. The same intermonomer contacts as in the orthorhombic crystals were observed in both hexagonal and tetragonal crystals, the X-ray structures of which were determined by the molecular-replacement method. These results suggest that the dimeric structure also exists under physiological conditions. These contacts, especially the subunit IVa–subunit I contact, in which the N-terminal portion of subunit IVa is placed on the surface of subunit I near the dioxygen-reduction site, indicate that the function of the bovine heart enzyme is likely to be controlled by perturbation of the monomer–monomer association.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Chester : International Union of Crystallography (IUCr)
    Journal of synchrotron radiation 6 (1999), S. 918-927 
    ISSN: 1600-5775
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: Proteins residing in the lipid bilayer of a membrane surrounding a biological compartment make it possible for the compartment to engage in specialized functions. Since the determination of the X-ray structure of the bacterial photoreaction centre, high-resolution structures for more than 15 integral membrane proteins have been elucidated, mainly by X-ray and partly by electron diffraction methods. The energy-conversion systems, namely those involving photosynthesis and respiration, contain various kinds of integral membrane proteins. The transmembrane parts of these membrane proteins fold into α-helices. Proton and electron transfer within the molecules have been inferred by inspecting the structures. Channels through which chemical substances are translocated selectively have important roles in various biological processes, such as mass transfer and signalling. Two structural architectures are known for the channels. One is an antiparallel β-barrel consisting of 14–22 strands and the other is α-helical consisting of eight to ten α-helices. Each channel has a structure suitable for selective transfer of a specific substance. Two types of anchoring architectures have been elucidated by the X-ray method. Prostaglandin H2 synthase-1 has helical anchors located with parallel orientation along and closely following the membrane surface. OmpA has an anchor domain arranged in the form of an antiparallel β-barrel consisting of eight strands.
    Type of Medium: Electronic Resource
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