Abstract
The radius of gyration (Rg) of bovine trypsinogen and β-trypsin was measured by an energy-dispersive X-ray technique as a function of Ca2+ or SO42− concentration; these results have been supplemented with measurements of association equilibrium constants of Ca2+ to its binding site(s) on both serine proteases and some of their adducts (with an effector and/or an inhibitor). As a whole, all information reported in the present work demonstrates that: (i) the strains exerted by different ions on these proteases produce diverse structural modifications; and (ii) at least in the case of Ca2+, the changes in Rg can be ascribed to the direct interaction of the binding site(s) on the protein matrix with the cation.
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