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1Author    Peter Gräber, Sathamm SaphonRequires cookie*
 Title    Conformational Changes of the Membrane-Bound ATPase of Bacterial Chromatophores Revealed by Fluorescence Changes of Fluorescamine-Labelled Coupling Factors  
 Abstract    The solubilized coupling factor (Ft) of Rps. sphaeroides chromatophores was allowed to react with fiuorescamine which led to a fluorescence labelled F t . After reconstitution with the depleted membranes the fluorescence-labelled Fj was shown to restore photophosphorylation in continuous light in a similar way to the non-labelled F t . In parallel, a decrease of the fluorescence emission of the labelled and reconstituted coupling factor was observed. The solubilized and labelled F x showed also a fluorescence decrease as the polarity of the medium was increased. In single turnover flashes the fluorescence change was found to be inhibited by an uncoupling agent such as FCCP. The kinetics of the change were sensitive to phosphorylating agents and to an "energy transfer inhibitor" such as venturicidin. It is suggested that the observed fluorescence changes reflect conformational changes of the ATPase enzyme complex. 
  Reference    Z. Naturforsch. 33c, 421—427 (1978); received March 28 1978 
  Published    1978 
  Keywords    Chromatophores Coupling Factors, Fluorescence-Labelling, Conformational Changes 
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 TEI-XML for    default:Reihe_C/33/ZNC-1978-33c-0421.pdf 
 Identifier    ZNC-1978-33c-0421 
 Volume    33 
2Author    S. J. Coughlan, U. SchreiberRequires cookie*
 Title    Light Induced Changes in the Conformation of Spinach Thylakoid Membranes as Monitored by 90° and 180° Scattering Changes: A Comparative Investigation  
 Abstract    A series o f investigations on light induced thylakoid m em brane conform ational changes has been carried out using scattering changes m easured either at 9 0 ° or 180° (transm ittance changes) as criteria for changes in membrane structure upon illum ination. T hese two phenom ena were found to react similarly to a range o f photosynthetic inhibitors, to changes in the ionic (M g2+, H +) concentration, and to have similar difference spectra. H owever, it was found possible to distinguish these two phenomena by the differences in the kinetics o f the light induced rise times. This could be shown most clearly using an A m inco D W 2 spectrophotom eter with the measuring beam deflected through 90° by front face mirrors. The dark decay tim e o f the two scattering changes was similar. These results are discussed in relation to the hypothesis that the light induced narrow angle 90° scattering response represents m icroconform ational m em brane changes in response to proton uptake, and the 180° scattering changes represent a m ixed response including changes in the stacking o f thylakoids. 
  Reference    Z. Naturforsch. 39c, 1120—1127 (1984); received August 6 1984 
  Published    1984 
  Keywords    Conformational Changes, Thylakoids, Scattering Changes, C om parison 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-1120.pdf 
 Identifier    ZNC-1984-39c-1120 
 Volume    39 
3Author    U. P. FringeliRequires cookie*
 Title      
  Reference    (Z. Naturforsch. 31c, 746 [1976]; received August 17 1976) 
  Published    1976 
  Keywords    Electron Microscopy, Radiation Damage, Polypeptide Monolayers, Infrared Dichroism, Conformational Changes 
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 TEI-XML for    default:Reihe_C/31/ZNC-1976-31c-0746_n.pdf 
 Identifier    ZNC-1976-31c-0746_n 
 Volume    31 
4Author    Agostina Congiu, Castellano"., Mario Barterib, Antonio Bianconi3, Fabio Bruni3, StefanoDella Longac, Corrado Paolinelli3Requires cookie*
 Title    Conformational Changes Involved in the Switch from Ovalbumin to S-Ovalbumin  
 Abstract    For the first time a comparative study on conformational differences between native oval­ bumin and its heat-stable form, called S-ovalbumin. using small angle x-ray scattering, is reported. To detect a different pathway in the folding mechanism of the two proteins, scatter­ ing m easurements have been performed on ovalbumin and S-ovalbumin denatured with dif­ ferent concentrations o f guanidine hydrochloride, and by heating the proteins at acid pH. The intensity scattering curves provide evidence that the intermediate states in the unfolding process are globular for both proteins while their compactness changes. The reported experi­ mental results suggest that the ovalbumin to S-ovalbumin transformation can be considered a protein-switch triggered by changes in the chemical conditions of the protein environment. Because the conform ational changes are likely to be of functional importance, we infer that the occurrence in vivo o f S-ovalbumin is thus determined by the transformation of oval­ bumin, with a functional role for embryonic development, into a new protein with a dif­ ferent function. 
  Reference    Z. Naturforsch. 51c, 379 (1996); received December 19 1995/February 6 1996 
  Published    1996 
  Keywords    Protein Folding, Conformational Change, Denatured State, Synchrotron Radiation, X-Ray Scattering 
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 TEI-XML for    default:Reihe_C/51/ZNC-1996-51c-0379.pdf 
 Identifier    ZNC-1996-51c-0379 
 Volume    51 
5Author    Corrado Paolinelli3, M. Ario Barterib, Federico Boffi3, Francesca Forastieri3, Maria Cristina, G. Audianob, StefanoDella Longac, AgostinaCongiu Castellano3Requires cookie*
 Title    Structural Differences of Ovalbumin and S-Ovalbumin Revealed by Denaturing Conditions  
 Abstract    We found, by circular dichroism and Raman spectroscopy measurements, that the second­ ary structure of the native ovalbumin and of its heat-stable form, called S-ovalbumin, is a probe of the structural differences between the two proteins. Small angle X-ray scattering and circular dichroism measurem ents perform ed on the two proteins under denaturing condi­ tions, with different concentrations of guanidine hydrochloride, show the changes of the tertiary and secondary structure and a different pathway in the unfolding process. These experimental data confirm that the conversion of native ovalbumin into S-ovalbumin is irreversible and reveal that the response of the two proteins to the same chemical environ­ ment is different. 
  Reference    Z. Naturforsch. 52c, 645—653 (1997); received February 10/June 20 1997 
  Published    1997 
  Keywords    X-Ray Scattering, Conformational Changes, Protein Folding, Synchrotron Radiation, Circular Dichroism, Protein Structure 
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 TEI-XML for    default:Reihe_C/52/ZNC-1997-52c-0645.pdf 
 Identifier    ZNC-1997-52c-0645 
 Volume    52 
6Author    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