Secondary structural changes in globular protein induced by a surfactant: Fourier self-deconvolution of FT-IR spectra

Journal of Biomolecular Structure & Dynamics
S B DevF Walder

Abstract

Conformational changes in ovalbumin, a globular protein, induced by an anionic surfactant, sodium dodecyl sulfate (SDS), have been monitored by an FT-IR spectrometer using ZnSe cylindrical internal reflection optics which allows high quality IR spectra to be obtained in water solution. The most notable change, on addition of SDS, occurs in the composite band of the Amide I absorption band and the vibrational frequency of the composite C = O bond shifts from 1639 cm-1 to 1652 cm-1. On the other hand, the position of the Amide II band remains fairly unchanged. Comparison of the various peak positions in the deconvoluted spectra for the native protein and the perturbed protein clearly shows the effect of SDS on the secondary structures of the protein. SDS unfolds the protein. It increases the helix content slightly. More importantly, it alerts the beta sheet structure, destroying it almost completely in the Amide I region, while retaining it in its neighbourhood. In the deconvoluted spectra of the perturbed protein, a band at 1531 cm-1 indicates generation of some beta turns. We used the second derivative of the deconvoluted spectra for fixing positions of minor peaks and shoulders. The results of this study indicate that the deco...Continue Reading

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Citations

Mar 1, 1986·Bioscience Reports·D C Lee, D Chapman
Jun 1, 1989·Journal of Biomedical Materials Research·T J LenkK K Chittur
Jan 29, 1988·Biochimica Et Biophysica Acta·W K Surewicz, H H Mantsch
Jan 17, 1986·Biochimica Et Biophysica Acta·J M OlingerR S Brody

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