Analytical ultracentrifugation is a free solution technique with no supplementary immobilization, columns or membranes required, and can be used to study self-association and hetero-interactions, stoichiometry, reversibility and interaction strength across a very large dynamic range (dissociation constants from 10−12 M to 10−1 M). In the present paper, we review some of the advances that have been made in the two different types of sedimentation experiment – sedimentation equilibrium and sedimentation velocity – for the analysis of protein–protein interactions and indicate how major complications such as thermodynamic and hydrodynamic non-ideality can be dealt with.

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