title: Insight into protein-protein interactions from analytical ultracentrifugation.
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.
authors.affiliation: National Centre for Macromolecular Hydrodynamics, University of Nottingham, Sutton Bonington, Leicestershire LE12 5RD, UK. steve.harding@nottingham.ac.uk
authors.forename: Stephen E
authors.initials: SE
authors.lastname: Harding
authors.forename: Arthur J
authors.initials: AJ
authors.lastname: Rowe
mesh_terms: D000818:Animals; D005591:Chemical Fractionation / Q000379:methods*; D011232:Chemical Precipitation; D006801:Humans; D025941:Protein Interaction Mapping / Q000379:methods* / Q000592:standards; D055503:Protein Multimerization; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013816:Thermodynamics; D014461:Ultracentrifugation / Q000379:methods
chemical_list: D011506:Proteins