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+,

We'd like to find out the impact of these ions on the
binding rate. We determine these rates with stopped-flow
fluorescence measurements.


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