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.
Circular_dichroism_and.pdf - Published Version
Restricted to Registered users only
Download (436Kb) | Request a copy
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|
|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|
Actions (login required)