Characterization of hydrodynamic changes upon cation-binding to proteins

Cations are specifically recognized by numerous proteins. Despite their small size, their specific interactions with highly charged residues allow them to induce significant conformational changes on their binding proteins. The protein conformational changes induced by cation binding may be very large, and in several cases appears to account for the complete folding of a protein and/or for the triggering of its oligomerization. These properties, which are essential for their function, can be studied with triple detection size-exclusion chromatography (SEC-TD) in combination with Analytical Ultracentrifugation (AUC).


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