title: Sedimentation equilibrium studies.
abstract: The reversible formation of protein-protein interactions plays a crucial role in many biological processes. In order to carry out a thorough quantitative characterization of these interactions, it is essential to establish the oligomerization state of the individual components first. The sedimentation equilibrium method is ideally suited to perform these studies because it allows a reliable, accurate, and absolute value of the solution molecular weight of a macromolecule to be obtained. This technique is independent of the shape of the macromolecule under investigation and allows the determination of equilibrium constants for a monomer-multimer self-associating system.
authors.affiliation: Division of Protein Structure, National Institute for Medical Research, London, England, UK.
authors.forename: Ian A
authors.initials: IA
authors.lastname: Taylor
authors.forename: John F
authors.initials: JF
authors.lastname: Eccleston
authors.forename: Katrin
authors.initials: K
authors.lastname: Rittinger
mesh_terms: D000818:Animals; D046911:Macromolecular Substances; D008970:Molecular Weight; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D014461:Ultracentrifugation / Q000295:instrumentation / Q000379:methods*
chemical_list: D046911:Macromolecular Substances; D011506:Proteins