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Please use this identifier to cite or link to this item: http://dspace.library.iitb.ac.in/jspui/handle/10054/3733

Title: Binding of 8-anilinonaphthalene sulfonate to dimeric and tetrameric concanavalin A: Energetics and its implications on saccharide binding studied by isothermal titration calorimetry and spectroscopy
Authors: BANERJEE, T
KISHORE, N
Keywords: molten globule state
heat-capacity
low ph
thermodynamics
fluorescence
proteins
nonpolar
surface
sites
probe
Issue Date: 2006
Publisher: AMER CHEMICAL SOC
Citation: JOURNAL OF PHYSICAL CHEMISTRY B, 110(13), 7022-7028
Abstract: The binding of 8-anilinonaphthalene sulfonate to concanavalin A has been investigated. Isothermal titration calorimetry (ITC) and circular dichroism studies have been performed under different experimental conditions to understand the binding quantitatively and evaluate contributions of different forces responsible for it. Isothermal titration calorimetric results of concanavalin A with ANS at pH 5.2 and 2.5, where it exists as a dimer, indicated binding heterogeneity and two classes of noninteracting sites. Enhancement of the binding constants from native to pH 2.5 suggests that the ANS binding is strongly influenced by the protein charge and the favorable alteration in the structure of concanavalin A as suggested by near-UV CD results. No binding was observed with the tetrameric form of concanavalin A, indicating shielding of sites due to dimerization of canonical dimers. The results have also demonstrated existence of a hydrophobic binding site that is distinct from the saccharide binding site.
URI: http://dx.doi.org/10.1021/jp0563179
http://dspace.library.iitb.ac.in/xmlui/handle/10054/3733
http://hdl.handle.net/10054/3733
ISSN: 1520-6106
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