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: Division of Molecular Structure, MRC National Institute for Medical Research, The Ridgeway Mill Hill, London, NW7 1AA, UK, itaylor@nimr.mrc.ac.uk.
authors: Ian A
authors: IA
authors: Taylor
authors: Katrin
authors: K
authors: Rittinger
authors: John F
authors: JF
authors: Eccleston
mesh_terms: D046911:Macromolecular Substances / Q000737:chemistry / Q000302:isolation & purification*; D008970:Molecular Weight; D025941:Protein Interaction Mapping / Q000379:methods*; D060066:Protein Interaction Maps; D012996:Solutions / Q000737:chemistry
chemical_list: D046911:Macromolecular Substances; D012996:Solutions