Sainania, Mohini N and Mishra, Vinod K and Gupta, Vidya S and Ranjekar, Prabhakar K (1992) Circular dichroism and 13C nuclear magnetic resonance spectroscopy of pennisetin from pearl millet. In: Plant Science, 83 (1). pp. 15-22.
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Abstract
The conformation and stability of pearl millet prolamin (pennisetin) were examined by using circular dichroism and C-13 nuclear magnetic resonance spectroscopy. The far UV spectrum of pennisetin in 70% (v/v) aqueous ethanol showed the presence of predominant alpha-helical structure and its occurrence in the alpha + beta class of protein. The far and near UV spectra of pennisetin in ethanol: trifluoroethanol also supported this observation. However pennisetin showed the presence of some helical structure in 8 M urea which is known to be a highly unordered structure forming solvent. A decrease in alpha helical content of native pennisetin was observed with rise in temperature from 5-75-degrees-C and this effect of temperature was found to be reversible. A C-13 NMR spectrum of pennisetin in 70% ethanol suggested a high degree of molecular mobility in ethanol. Comparison of the cross polarization spectrum with the single pulse excitation spectrum suggested pennisetin to be a heterogeneous protein.
Item Type: | Journal Article |
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Publication: | Plant Science |
Publisher: | Elsevier science |
Additional Information: | Copyright of this article belongs to Elsevier science. |
Keywords: | Pearl millet;pennisetin;circular dichroism;nuclear magnetic resonance spectroscopy. |
Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
Date Deposited: | 25 Jan 2011 06:28 |
Last Modified: | 25 Jan 2011 06:28 |
URI: | http://eprints.iisc.ac.in/id/eprint/35134 |
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