Protein-protein and ligand-protein interactions studied by analytical ultracentrifugation.
All biological processes involve molecular interactions that result in either binding, self-association, or hetero-associations of one form or another. It is important to understand that no interactions are completely all-or-none. Some approach all-or-none only when there is strong positive cooperativity. Examples will be given of typical biomolecular interactions and their expected dependence on concentration, in order to point out the relatively wide range of concentration over which these types of phenomena take place. This chapter is concerned both with the binding of low-molecular-weight ligands to macromolecules as well as interactions between macromolecules using analytical ultracentrifugation (AUC) as a tool for measuring association properties of these systems. The theory of sedimentation of both ideal and nonideal interacting and noninteracting systems is discussed. Examples are given of each type of system along with a discussion of how each type of system can be analyzed. Several methods of data analysis are discussed.
Stafford
Walter F
WF
Boston Biomedical Research Institute, Watertown, MA, USA.
D008024:Ligands; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*; D014461:Ultracentrifugation / Q000379:methods
D008024:Ligands; D011506:Proteins