Gupta, Garima and Sinha, Sharmistha and Surolia, Avadhesha (2008) Unfolding energetics and stability of banana lectin. In: Proteins: Structure, Function, and Bioinformatics, 72 (2). pp. 754-760.
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The unfolding pathway of banana lectin from Musa paradisiaca was determined by isothermal denaturation induced by the chaotrope GdnCl. The unfolding was found to be a reversible process. The data obtained by isothermal denaturation provided information on conformational stability of banana lectin. The high values of DG of unfolding at various temperatures indicated the strength of intersubunit interactions.It was found that banana lectin is a very stable and denatures at high chaotrope concentrations only. The basis of the stability may be attributed to strong hydrogen bonds of the order 2.5–3.1 \AA at the dimeric interface along with the presence of water bridges. This is perhaps very unique example in proteins where subunit association is not a consequence of the predominance of hydrophobic interactions.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to John Wiley & Sons.|
|Keywords:||banana lectin (banlec);chaotropic denaturation;two-state unfolding;free energy DG;hydrogen bonds.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||21 Jul 2008|
|Last Modified:||19 Sep 2010 04:47|
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