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A new polarized target for neutron scattering studies on biomolecules: first results from apoferritin and the deuterated 50S subunit of ribosomes (1992)

Knop, W. ; Hirai, M. ; Schink, H. J. ; [et al.]

Copenhagen : International Union of Crystallography (IUCr)

Applied crystallography online 25 (1992), S. 155-165

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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

URL: http://dx.doi.org/10.1107/S0021889891011093

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Ribosomal proteins (1972)

Crichton, R. R. ; Wittmann, H. G.

Springer

Molecular genetics and genomics 114 (1972), S. 95-105

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ISSN: 1617-4623

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Summary The susceptibility of 30S and 50S ribosomal subunits and of intact 70S ribosomes from E. coli to digestion with trypsin has been analysed by 2-dimensional electrophoresis. A classification of the ribosomal proteins on the basis of their rate of digestion by trypsin is proposed, and it is shown that it is possible to remove proteins by this method in a stepwise manner. The suitability of this method as a probe of the ribosomal conformation is discussed and compared with results from other investigations.