2,2,2-Trifluoroethanol-Induced Structural Change of Peanut Agglutinin at Different pH: A Comparative Account

Dev, Sagarika and Khan, RH and Surolia, Avadhesha (2006) 2,2,2-Trifluoroethanol-Induced Structural Change of Peanut Agglutinin at Different pH: A Comparative Account. In: IUBMB Life (International Union of Biochemistry and Molecular Biology: Life), 58 (8). pp. 473-479.

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Abstract

Peanut Agglutinin (PNA) is a legume lectin with a unique open quarternary structure. It is a homotetrameric protein, the monomeric subunit of which is made up of $3\hspace{2mm}{\beta}$ sheets. The structural change in this protein has been induced by 2,2,2-trifluoroethanol (TFE) at two different pH. At neutral pH, PNA exists as a homotetramer, while at pH 2.5, it is known to dissociate to a dimer. The effect of TFE has been studied at both the pH by intrinsic tryptophan fluorescence, far and near UV Circular Dichroism, ANS binding and dynamic light scattering. At low pH, 15% TFE is found to induce a molten globule like state that shows maximum ANS binding. Increasing concentration of TFE increases a helical content and the compactness of the protein. The compact PNA at higher concentration of TFE is structurally different from the native structure. The effect of TFE at neutral pH on PNA is somewhat different from that observed at low pH. TFE does not induce molten globule like state at this pH. The detailed study of the structural change of PNA by TFE has been presented.

Item Type:	Journal Article
Publication:	IUBMB Life (International Union of Biochemistry and Molecular Biology: Life)
Publisher:	Taylor and Francis
Additional Information:	Copyright of this article belongs to Taylor and Francis.
Keywords:	PNA;Different pH;Trifuoroethanol;Secondary structural change.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	26 Nov 2007
Last Modified:	19 Sep 2010 04:31
URI:	http://eprints.iisc.ac.in/id/eprint/8658

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