ISSN:
0006-3525
Keywords:
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
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.
Additional Material:
2 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bip.1979.360180505
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