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1997 (1)
1Author    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