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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Conference Article| July 26 2010
Insight into protein–protein interactions from analytical ultracentrifugation
Stephen E. Harding;
Stephen E. Harding 1
1National Centre for Macromolecular Hydrodynamics, University of Nottingham, Sutton Bonington, Leicestershire LE12 5RD, U.K.
1To whom correspondence should be addressed (email firstname.lastname@example.org).
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Publisher: Portland Press Ltd
Received: May 11 2010
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2010 Biochemical Society
Stephen E. Harding, Arthur J. Rowe; Insight into protein–protein interactions from analytical ultracentrifugation. Biochem Soc Trans 1 August 2010; 38 (4): 901–907. doi: https://doi.org/10.1042/BST0380901
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