Gupta, Garima ; Sinha, Sharmistha ; Surolia, Avadhesha (2008) Unfolding energetics and stability of banana lectin Proteins: Structure, Function, and Bioinformatics, 72 (2). pp. 754-760. ISSN 0887-3585
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Official URL: http://onlinelibrary.wiley.com/doi/10.1002/prot.21...
Related URL: http://dx.doi.org/10.1002/prot.21961
Abstract
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 ΔG 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 Å 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: | Article |
|---|---|
| Source: | Copyright of this article belongs to John Wiley and Sons. |
| Keywords: | Banana Lectin (Banlec); Chaotropic Denaturation; Two-state Unfolding; Free Energy ΔG; Hydrogen Bonds |
| ID Code: | 56652 |
| Deposited On: | 25 Aug 2011 10:26 |
| Last Modified: | 25 Aug 2011 10:26 |
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