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The folding and binding kinetics of two homologous proteins: alpha-lactalbumin and lysozyme. Katrien Noyelle, University of Leuven, Campus Kortrijk E. Sabbelaan 53 8500 Kortrijk BELGIUM So far, we concentrated on the folding of two proteins : bovine alpha-lactalbumin (BLA - a Ca2+-binding protein) and human lysozyme. Despite their homologous structure, these two proteins differ profoundly in their unfolding behaviour: lysozymes undergo two-state thermal denaturation while the Ca2+-free form of BLA adopts a 'molten globule'-state. Apart from the folding problem, we are also interested in the kinetics of binding of several metal ions to BLA. As already mentioned, BLA is a Ca2+-binding protein but it can also bind (to a minor extent) other metal ions such as Mn2+, Mg2+, Sr2+... We'd like to find out the impact of these ions on the binding rate. We determine these rates with stopped-flow fluorescence measurements. ## Back to the list of abstracts