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'Small Angle X Ray Scattering' in keywords
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1988 (1)
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1978 (1)
1Author    H. Wawra, H. Buschmann, H. Formanek, S. FormanekRequires cookie*
 Title    Strukturuntersuchung mit Röntgenbeugungsmethoden an Lipopolysacchariden von Salmonella minnesota Mutanten S SF 1111 und R 595 SF 1167 Structural Investigations on Lipopolysaccharides of Mutants S SF 1111 and R 595 SF 1167 of Salmonella minnesota  
 Abstract    The lipolysaccharides of two m utants of Salmonella minnesota with known chemical structure were investigated by X-ray methods. Both thickness of the lipopolysaccharide layer and arrange­ ment of the m olecular components could be estim ated. Using these informations a space-filling model of the structure was built. 
  Reference    Z. Naturforsch. 34c, 171 (1979); eingegangen am 27. Dezember 1978 
  Published    1979 
  Keywords    Small-Angle-X-Ray Scattering, Bacterial Cell W all, Lipopolysaccharides 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0171.pdf 
 Identifier    ZNC-1979-34c-0171 
 Volume    34 
2Author    Peter Zipper, Helmut DurchschlagRequires cookie*
 Title    Small-Angle X-Ray Scattering on Malate Synthase from Baker's Yeast Considerations on the Effects of Bound Ligands  
  Reference    Z. Naturforsch. 33c, 504 (1978); received June 12 1978 
  Published    1978 
  Keywords    M alate Synthase, Small-Angle X-Ray Scattering, Structural Changes on Ligand Binding, M odels for Enzyme-Substrate Complexes, Binding Site 
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 TEI-XML for    default:Reihe_C/33/ZNC-1978-33c-0504.pdf 
 Identifier    ZNC-1978-33c-0504 
 Volume    33 
3Author    P. M. Abuja, I. PilzRequires cookie*
 Title    Investigation of Ribulose-1,5-bisphosphate Carboxylase-Oxygenase from Tobacco by Small Angle X-Ray Scattering: A Structural Model for the Enzyme in Solution  
 Abstract    The quaternary structure of ribulose-l,5-bisphosphate carboxylase/oxygenase from tobacco (Nicotiana tabacum) was investigated in solution by means of small angle X-ray scattering. The most important molecular parameters as the radius of gyration (Rg) and the maximum diameter (Dmax) were determined. Both the active and the inactive form of the enzyme were measured at 5 °C and at 20 °C. A more distinct difference in size could be detected between the inactive forms at these two temperatures (Rg = 4.80 nm (5 °C) and 4.68 nm (20 °C)) than between the active forms (Rg = 4.73 nm and 4.69 nm). The maximum diameters were determined to be 13.1 nm for the inactive form at 5 °C and 12.8 nm for the other forms. A model is proposed consisting of eight large and eight small subunits arranged in the way that seems to be typical for this enzyme in higher plants. 
  Reference    Z. Naturforsch. 43c, 373—376 (1988); received December 21 1987/February 15 1988 
  Published    1988 
  Keywords    Small-Angle X-Ray Scattering, Solution Structure, Ribulose-l, 5-bisphosphate Carboxylase/ Oxygenase, Conformational Change, Temperature Effect 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0373.pdf 
 Identifier    ZNC-1988-43c-0373 
 Volume    43 
4Author    Peter ZipperRequires cookie*
 Title    Small-Angle X-Ray Scattering Studies on the X-Ray Induced Aggregation of Malate Synthase Computer Simulations and Models  
 Abstract    Malate synthase undergoes an X-ray induced aggregation which can be monitored in situ by small-angle X-ray scattering; the analysis o f scattering curves, taken at subsequent stages o f aggregation, has led to the establishment of a tentative model for an aggregation in two dimensions (Zipper and Durchschlag (1980) Rad. and Environm. Biophys., in press). This model was checked by comparison o f appropriate theoretical curves with the experi­ mental curves. The theoretical scattering curves for this comparison were obtained by weighted averaging over the scattering curves calculated for various species o f hypothetical aggregates. Based on the approximation o f the unaggregated enzyme particle by an oblate cylinder, the aggregates were assumed to be composed of 2, 3, 4 or 6 of such cylinders, associated side-by-side in one and later on in two linear rows. The weight fractions o f the species were chosen so, that an optimum fit of the experimental mean radii o f gyration and mean degrees o f aggregation was achieved. The distance distribution functions calculated for the model are very similar to the functions derived from the scattering experiment. Cross-section Guinier plots o f the scattering curves of the model reveal the occurrence o f one and later on o f two pseudo cross-section factors similar to those observed in the experimental scattering curves. The pseudo thickness factor of the model of the unaggregated particle is found to be retained in the model curves for all stages of aggregation. From these results it can be concluded that the model for the aggregation process is essentially consistent with the scattering behaviour of the aggregating enzyme. Small differences between the theoretical and experimental curves may be explained by the idealizations o f the model. The comparison of theoretical curves for alternative models, assuming aggregation in three dimen­ sions, suggests that these models are unlikely, though small amounts o f three-dimensional aggregates cannot be ruled out completely. 
  Reference    Z. Naturforsch. 35c, 890—901 (1980); received November 12 1979/July 14 1980 
  Published    1980 
  Keywords    Malate Synthase, Small-Angle X-Ray Scattering, X-Ray Induced Aggregation, Computer Simula­ tions, Models for the Aggregation Process 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0890.pdf 
 Identifier    ZNC-1980-35c-0890 
 Volume    35