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1996[X]
1Author    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