Binding of alkylsulfonate ligands to bovine β-lactoglobulin: Effects on protein thermal unfolding

The effects caused by alkylsulfonate ligands (ALn), characterized by a similar sulfonate head and a progressively longer hydrocarbon tail, on the thermal unfolding of beta-lactoglobulin (β-LG) were examined by using UV-difference spectroscopy at 293 nm (ΔAbs293) and by following the external quenching of the intrinsic protein fluorescence by acrylamide. At pH 6.8, the interaction with the different ALn added promoted a stabilization of the protein structure in the following sense: AL8更多