109 research outputs found

    Thermoeconomic Analysis of a Solar Dish Micro Gas-turbine Combined-cycle Power Plant

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    AbstractA novel solar power plant concept is presented, based on the use of a coupled network of hybrid solar-dish micro gas-turbines, driving a centralized heat recovery steam generator and steam-cycle, thereby seeking to combine the high efficiency of the solar dish collector with a combined-cycle power block. A 150 MWe solar power plant was designed based on this concept and compared with both a conventional combined-cycle power plant and a hybrid solar-tower combined-cycle. The solar dish combined-cycle power plant could reach higher levels of solar integration than other concepts but was shown to be more expensive with current technology; solar electricity costs are double those of the hybrid solar-tower combined cycle

    Understanding hierarchy and functions of bone using scanning x-ray scattering methods

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    International audienceBiological materials are often hierarchically structured from the nanometer to the macroscopic scale. Specific characterization methods are needed to characterize the structures at these different length scales. This chapter reviews -based on the example of bone- the use of X-ray scattering methods to explore representative and quantitative structure information as well as structure-function relations in hierarchically structured biological materials. X-ray scattering techniques are particularly well suited for the characterization of the form and organization of organic and inorganic components in those materials. When nanometer-sized structures are exposed to X-rays, details of the internal material structure can be revealed by the analysis of the resulting interference patterns. Fundamental aspects of wide and small angle X-ray scattering (WAXS and SAXS) are discussed with specific focus on bone studies. An important field of research using X-ray scattering techniques, is the in situ combination with mechanical testing, which allows investigating changes in structure under specific loading conditions. Another common application is the structural study of heterogeneities or local structures within a sample using a narrow focused X-ray beam. Furthermore, in scanning mode, where the specimen is displaced step by step across a microbeam while collecting a SAXS/WAXS pattern at each step, complex structural maps of the sample can be derived. A natural extension of the method toward imaging is described in the context of X-ray imaging with scattering contrast

    Structural purity of magnetite nanoparticles in magnetotactic bacteria

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    Magnetosome biomineralization and chain formation in magnetotactic bacteria are two processes that are highly controlled at the cellular level in order to form cellular magnetic dipoles. However, even if the magnetosome chains are well characterized, controversial results about the microstructure of magnetosomes were obtained and its possible influence in the formation of the magnetic dipole is to be specified. For the first time, the microstructure of intracellular magnetosomes was investigated using high-resolution synchrotron X-ray diffraction. Significant differences in the lattice parameter were found between intracellular magnetosomes from cultured magnetotactic bacteria and isolated ones. Through comparison with abiotic control materials of similar size, we show that this difference can be associated with different oxidation states and that the biogenic nanomagnetite is stoichiometric, i.e. structurally pure whereas isolated magnetosomes are slightly oxidized. The hierarchical structuring of the magnetosome chain thus starts with the formation of structurally pure magnetite nanoparticles that in turn might influence the magnetic property of the magnetosome chains

    Preparative SDS PAGE as an Alternative to His–Tag Purification of Recombinant Amelogenin

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    Recombinant protein technology provides an invaluable source of proteins for use in structure-function studies, as immunogens and in the development of therapeutics. Recombinant proteins are typically engineered with “tags” that allow the protein to be purified from crude host cell extracts using affinity based chromatography techniques. Amelogenin is the principal component of the developing enamel matrix and a frequent focus for biomineralisation researchers. Several groups have reported the successful production of recombinant amelogenins but the production of recombinant amelogenin free of any tags, and at single band purity on silver stained SDS PAGE is technically challenging. This is important, as rigorous structure-function research frequently demands a high degree of protein purity and fidelity of protein sequence. Our aim was to generate His-tagged recombinant amelogenin at single band purity on silver stained SDS PAGE for use in functionality studies after His-tag cleavage. An acetic acid extraction technique (previously reported to produce recombinant amelogenin at 95% purity directly from E. coli) followed by repeated rounds of nickel column affinity chromatography, failed to generate recombinant amelogenin at single band purity. This was because following an initial round of nickel column affinity chromatography, subsequent cleavage of the His-tag was not 100% efficient. A second round of nickel column affinity chromatography, used in attempts to separate the cleaved His-tag free recombinant from uncleaved His-tagged contaminants, was still unsatisfactory as cleaved recombinant amelogenin exhibited significant affinity for the nickel column. To solve this problem, we used preparative SDS PAGE to successfully purify cleaved recombinant amelogenins to single band purity on silver stained SDS PAGE. The resolving power of preparative SDS PAGE was such that His-tag based purification of recombinant amelogenin becomes redundant. We suggest that acetic acid extraction of recombinant amelogenin and subsequent purification using preparative SDS PAGE provides a simple route to highly purified His-tag free amelogenin for use in structure-function experiments and beyond

    Amelogenin Supramolecular Assembly in Nanospheres Defined by a Complex Helix-Coil-PPII Helix 3D-Structure

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    Tooth enamel, the hardest material in the human body, is formed within a self-assembled matrix consisting mostly of amelogenin proteins. Here we have determined the complete mouse amelogenin structure under physiological conditions and defined interactions between individual domains. NMR spectroscopy revealed four major amelogenin structural motifs, including an N-terminal assembly of four α-helical segments (S9-V19, T21-P33, Y39-W45, V53-Q56), an elongated random coil region interrupted by two 310 helices (∌P60-Q117), an extended proline-rich PPII-helical region (P118-L165), and a charged hydrophilic C-terminus (L165-D180). HSQC experiments demonstrated ipsilateral interactions between terminal domains of individual amelogenin molecules, i.e. N-terminal interactions with corresponding N-termini and C-terminal interactions with corresponding C-termini, while the central random coil domain did not engage in interactions. Our HSQC spectra of the full-length amelogenin central domain region completely overlapped with spectra of the monomeric Amel-M fragment, suggesting that the central amelogenin coil region did not involve in assembly, even in assembled nanospheres. This finding was confirmed by analytical ultracentrifugation experiments. We conclude that under conditions resembling those found in the developing enamel protein matrix, amelogenin molecules form complex 3D-structures with N-terminal α-helix-like segments and C-terminal PPII-helices, which self-assemble through ipsilateral interactions at the N-terminus of the molecule

    Amelogenin Nanoparticles in Suspension: Deviations from Spherical Shape and pH-Dependent Aggregation

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    It is well-known that amelogenin self-assembles to form nanoparticles, usually referred to as amelogenin nanospheres, despite the fact that not much is known about their actual shape in solution. In the current paper, we combine SAXS and DLS to study the three-dimensional shape of the recombinant amelogenins rP172 and rM179. Our results show for the first time that amelogenins build oblate nanoparticles in suspension using experimental approaches that do not require the proteins to be in contact with a support material surface. The SAXS studies give evidence for the existence of isolated amelogenin nano-oblates with aspect ratios in the range of 0.45-0.5 at pH values higher than pH 7.2 and show an aggregation of these nano-oblates at lower pH values. The role of the observed oblate shape in the formation of chain-like structures at physiological conditions is discussed as a key factor in the biomineralization of dental enamel
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