| | 1 | 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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| ZNC-1997-52c-0645 | | | | Volume
| 52 | |
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