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  • 1
    Electronic Resource
    Electronic Resource
    Small- and wide-angle X-ray scattering investigations of injection-moulded polypropylene (1991)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 24 (1991), S. 702-708 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: The layered structure in 2 mm thick discs injection moulded from industrial polypropylene (PP) was studied by scanning the cross section of the mouldings by means of small- and wide-angle X-ray scattering (SAXS and WAXS), using a Kratky collimation system for position-resolved quantitative scattering measurements in both angular domains. The registration of so-called scattering profiles of the mouldings and a texture analysis of the WAXS profiles were established as novel approaches for studying the cross-section architecture. The results of the investigations comprise statements on the preferential orientation and the local distribution of α- and β-PP in different layers of the cross sections, on crystallite sizes and on the behaviour of individual layers in tensile tests.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889891001917
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Small-angle X-ray study on the structure of ribulose-1,5-bisphosphate carboxylase-oxygenase from Rhodospirillum rubrum (1986)
    Springer
    European biophysics journal 14 (1986), S. 93-96 
    Details
    ISSN: 1432-1017
    Keywords: Small-angle X-ray scattering ; solution structure ; ribulose-1,5-bisphosphate ; carboxylase/oxygenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract The quaternary structure of ribulose-1,5-bisphosphate carboxylase-oxygenase (rubisco) from Rhodospirillum rubrum, an enzyme consisting of two large subunits, L2, was investigated by small-angle X-ray scattering. In the presence of HCO 3 - and Mg2+, rubisco is in the active state and displays a radius of gyration of 2.96 nm, a maximum diameter of 9.5 nm and a volume of 170 nm3. A model is presented where the subunits are arranged back-to-back, rotated relative to each other by 90°, and shifted by 1.3 nm. Upon inactivation by removal of HCO 3 - and Mg2+, the model swells slightly without any distinct changes in configuration. This contrasts with our previous observations with rubisco from Alcaligenes eutrophus, an enzyme composed of small (S) and large (L) subunits, L8S8, where inactivation gives rise to substantial changes in configuration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00263065
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Structural and functional domains of cellobiohydrolase I from trichoderma reesei (1988)
    Springer
    European biophysics journal 15 (1988), S. 339-342 
    Details
    ISSN: 1432-1017
    Keywords: Cellobiohydrolase I ; core CBH I ; small angle X-ray scattering ; model for solution structure ; functional-structural domains
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Limited proteolysis (papain) of the cellobiohydrolase I (CBH I, 65 kDa) from Trichoderma reesei led to the seperation of two functional domains: a core protein (55 kDa) containing the active site, and a C-terminal glycopeptide (10 kDa) implicated in binding to the insoluble matrix (cellulose). The quaternary structures of the intact CBH I and its core in solution are now compared by small angle X-ray scattering (SAXS) measurements. The molecular parameters derived for the core (Rg=2.09 nm, Dmax=6.5 nm) and for the intact enzyme (Rg=4.27 nm, Dmax=18 nm) indicate very different shapes. The resulting models show a “tadpole”-like structure for the intact enzyme where the isotropic part coincides with the core protein and the flexible tail part should be identified with the C-terminal glycopeptide. Thus in this enzyme, functional differentiation is reflected in structural peculiarities.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00254721
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    Paper (German National Licenses)
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