title: Measuring protein-protein interactions by equilibrium sedimentation.
abstract: This unit describes basic principles and practice of sedimentation equilibrium analytical ultracentrifugation for the study of reversible protein interactions, such as the characterization of self-association, heterogeneous association, and binding stoichiometry, as well as the determination of association constants. Advanced tools such as mass conservation analysis, multiwavelength analysis, and global analysis are introduced and discussed in the context of the experimental design. A detailed protocol guiding the investigator through the experimental steps and the data analysis is available as an internet resource.
authors.affiliation: National Institutes of Health, Bethesda, Maryland.
authors.forename: Andrea
authors.initials: A
authors.lastname: Balbo
authors.affiliation: National Institutes of Health, Bethesda, Maryland.
authors.forename: Patrick H
authors.initials: PH
authors.lastname: Brown
authors.affiliation: University of Connecticut, Storrs, Connecticut.
authors.forename: Emory H
authors.initials: EH
authors.lastname: Braswell
authors.affiliation: University of Connecticut, Storrs, Connecticut.
authors.forename: Peter
authors.initials: P
authors.lastname: Schuck
mesh_terms: D000818:Animals; D002623:Chemistry Techniques, Analytical / Q000295:instrumentation / Q000379:methods; D006801:Humans; D046911:Macromolecular Substances / Q000302:isolation & purification / Q000378:metabolism; D008962:Models, Theoretical; D011485:Protein Binding; D012107:Research Design; D012984:Software; D013223:Statistics as Topic / Q000379:methods; D013816:Thermodynamics; D014461:Ultracentrifugation / Q000295:instrumentation / Q000379:methods
chemical_list: D046911:Macromolecular Substances