Structural differences of ovalbumin and S-ovalbumin revealed by denaturing conditions.
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.
Paolinelli
C
C
Dipartimento di Fisica and INFM, Università La Sapienza, Roma, Italy.
Barteri
M
M
Boffi
F
F
Forastieri
F
F
Congiu Gaudiano
M
M
Della Longa
S
S
Castellano
A C
AC
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
C104026:S-ovalbumin; D010047:Ovalbumin; D019791:Guanidine