Influence of experimental conditions and Trp mutations on the stability and the folding characteristics of goat α-lactalbumin

In this study it is shown that small differences in local sequence or in the nature of local interactions can exert significant influence on the formation and properties of equilibrium and kinetic intermediate states and can play a determining role in the evolution of the folding process. Goat α-lactalbumin was taken as model system. Experimental conditions were changed by decalcification or by varying the pH. The influence of individual amino acids was studied by the mutation of the tryptophan residue at position 60 or/and position 118.