title: Structural differences of ovalbumin and S-ovalbumin revealed by denaturing conditions.
abstract: We found, by circular dichroism and Raman spectroscopy measurements, that the secondary 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 measurements performed on the two proteins under denaturing conditions, 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 environment is different.
authors.affiliation: Dipartimento di Fisica and INFM, Università La Sapienza, Roma, Italy.
authors.forename: C
authors.initials: C
authors.lastname: Paolinelli
authors.forename: M
authors.initials: M
authors.lastname: Barteri
authors.forename: F
authors.initials: F
authors.lastname: Boffi
authors.forename: F
authors.initials: F
authors.lastname: Forastieri
authors.forename: M
authors.initials: M
authors.lastname: Congiu Gaudiano
authors.forename: S
authors.initials: S
authors.lastname: Della Longa
authors.forename: A C
authors.initials: AC
authors.lastname: Castellano
mesh_terms: D000818:Animals; D002645:Chickens; D019791:Guanidine; D006358:Hot Temperature; D010047:Ovalbumin / Q000737:chemistry*; D011487:Protein Conformation; D011489:Protein Denaturation; D012542:Scattering, Radiation; D013059:Spectrum Analysis, Raman / Q000379:methods; D013816:Thermodynamics
chemical_list: C104026:S-ovalbumin; D010047:Ovalbumin; D019791:Guanidine