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1997 (1)
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1Author    W. Altraud, Folkhard*. Daniela, C. Hristm, Ann, W. Erner, G. Eercken, Ernst Knörzer, MichelH J Koch, Erika Mosler, HediN. Emetschek-Gansler, Theobald NemetschekRequires cookie*
 Title    Twisted Fibrils are a Structural Principle in the Assembly of Interstitial Collagens, Chordae Tendineae Included  
 Abstract    X-ray diffraction analysis of connective tissue samples, which contain type I and type III collagen shows that twisted collagen fibrils are a general principle of assembly. The occurrence of twisted fibrils in native wet Chordae tendineae, skin and Aorta is combined with a shorter axial periodicity of about 65 nm. This shorter D period is shown to be directly related to the tilt of the molecules, which have to be curved to build-up twisted fibrils. 
  Reference    Z. Naturforsch. 42c, 1303—1306 (1987); received October 5. 1987 
  Published    1987 
  Keywords    Collagen, Skin, Aorta, Chordae tendineae, X-Ray Diffraction, Synchrotron Radiation 
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 TEI-XML for    default:Reihe_C/42/ZNC-1987-42c-1303.pdf 
 Identifier    ZNC-1987-42c-1303 
 Volume    42 
2Author    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 
3Author    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