ZfN: Search Results

1	Author	Agostina Congiu, Castellano"., Mario Barterib, Antonio Bianconi3, Fabio Bruni3, StefanoDella Longac, Corrado Paolinelli3	Requires 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

2	Author	Corrado Paolinelli3, M. Ario Barterib, Federico Boffi3, Francesca Forastieri3, Maria Cristina, G. Audianob, StefanoDella Longac, AgostinaCongiu Castellano3	Requires 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