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  • Electronic Resource  (2)
  • 1990-1994  (1)
  • 1975-1979  (1)
  • 1992  (1)
  • 1977  (1)
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  • Electronic Resource  (2)
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  • 1990-1994  (1)
  • 1975-1979  (1)
Year
  • 1992  (1)
  • 1977  (1)
  • 1978  (2)
  • 1
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: A new polarized target for neutron scattering has been designed by CERN and tested successfully using the reactor FRG-1 at the GKSS Research Centre. The nuclear spins are aligned with respect to the external field – parallel or antiparallel – by dynamic nuclear polarization (DNP). To avoid absorption of neutrons by 3He, the frozen solutions of biomolecules are immersed in liquid 4He which in turn is thermally coupled to the cooling mixture of 3He/4He of the dilution refrigerator. Compared with earlier experiments where the sample had been cooled directly by 3He, the rate of detectable neutrons increased by a factor of 30. Another factor of 30 is due to the installation of the cold source and the beryllium reflector in FRG-1. Polarized neutron scattering from apoferritin in deuterated solvent shows that the proton spin polarization is homogeneous in apoferritin molecules. After saturation of proton nuclear magnetic resonance (NMR), polarized neutron scattering is dominated by deuteron spin contrast. With the deuterated large subunit of E. coli ribosomes, three different basic scattering functions are derived from spin-contrast variation, reflecting the known scattering-length-density distribution of the architecture of rRNA and ribosomal proteins. The planned in situ structure determination of a mRNA fragment is discussed in the light of the present results.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 152 (1977), S. 253-257 
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A new photoactivable reagent is described, which allows the formation of RNA-protein crosslinks via disulfide bridges in combination with mercaptobutyrimidate. The reconstituted L24 protein-23S RNA complex from the large subunit of E. coli ribosomes has been used as a model system for the cross-linking. The main advantages of the reagent are the absence of U.V. generated cross-links, since photoactivation is carried out at 360 nm, on one hand and the ease of cleavage of the cross-link by mild reduction (β-mercaptoethanol) on the other.
    Type of Medium: Electronic Resource
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