A Raman difference spectroscopic investigation of ovalbumin and S-ovalbumin
| Autor: | Yoshio Tomimatsu, Saima Kint |
|---|---|
| Rok vydání: | 1979 |
| Předmět: |
chemistry.chemical_classification
Aqueous solution biology Stereochemistry Organic Chemistry Biophysics S-ovalbumin Peptide General Medicine Antiparallel (biochemistry) Biochemistry Biomaterials Crystallography Ovalbumin symbols.namesake chemistry biology.protein symbols Chemical stability Raman spectroscopy |
| Zdroj: | Biopolymers. 18:1073-1079 |
| ISSN: | 1097-0282 0006-3525 |
| DOI: | 10.1002/bip.1979.360180505 |
| Popis: | Raman spectra from 800 to 1850 cm−1 of aqueous solutions of ovalbumin and its more heat-stable form, S-ovalbumin, are presented. A Raman difference spectrum (ovalbumin minus S-ovalbumin) shows differences in intensity in the amide I and III regions. These intensity differences lead us to postulate that the conversion of ovalbumin to S-ovalbumin involves a conformation change of a small part (∼3–4%) of the protein from α-helix to antiparallel β-sheet geometry. This small difference in the three-dimensional arrangement of the peptide chain may contribute to the large difference in the thermodynamic stability between ovalbumin and S-ovalbumin. |
| Databáze: | OpenAIRE |
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