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Updated: Jan 20, 2026

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
Published on: November 7, 2013
Insight into protein-protein interactions from analytical ultracentrifugation
Stephen E Harding1, Arthur J Rowe
1National Centre for Macromolecular Hydrodynamics, University of Nottingham, Sutton Bonington, Leicestershire LE12 5RD, UK. steve.harding@nottingham.ac.uk
Abstract:
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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