Dev, Sagarika and Nirmala, Devi K and Sinha, Sharmistha and Surolia, Avadhesha (2006) Thermodynamic analysis of three state denaturation of Peanut Agglutinin. In: IUBMB Life, 58 (9). pp. 549-555.
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Peanut Agglutinin (PNA) is a homotetrameric protein with a very unusual open quaternary structure. During denaturation, it first dissociates into a molten globule like state, which subsequently undergoes complete denaturation. Urea denaturation of PNA at neutral pH has been studied by intrinsic fluorescence spectroscopy and has been fitted to a three state model, A(4) double left right arrow 4I double left right arrow 4U, to get all the relevant thermodynamic parameters. Urea denaturation leads to continuous red shift of wavelength maxima. The molten globule like state is formed in a short range of urea concentration. Refolding of the denatured PNA has been attempted by intrinsic fluorescence study. Refolding by instantaneous dilution shows the occurrence of the formation of an intermediate at a relatively rapid rate, within few seconds. The transition from PNA tetramer to molten globule like state is found to have a Delta G value of similar to 33 kcal/mole while it is similar to 8 kcal/mole for the transition from molten globule like state to a completely denatured state. This in turn indicates that the tetramerization in PNA contributes significantly to the stability of the oligomer.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to John Wiley and Sons.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||21 May 2010 06:33|
|Last Modified:||19 Sep 2010 06:01|
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