title: Characterizing protein-protein interactions by sedimentation velocity analytical ultracentrifugation.
abstract: This unit introduces the basic principles and practice of sedimentation velocity analytical ultracentrifugation for the study of reversible protein interactions, such as the characterization of self-association, heterogeneous association, multi-protein complexes, binding stoichiometry, and the determination of association constants. The analytical tools described include sedimentation coefficient and molar mass distributions, multi-signal sedimentation coefficient distributions, Gilbert-Jenkins theory, different forms of isotherms, and global Lamm equation modeling. Concepts for the experimental design are discussed, and a detailed step-by-step protocol guiding the reader through the experiment and the data analysis is available as an Internet resource.
authors.affiliation: National Institutes of Health, Bethesda, Maryland.
authors.forename: Patrick H
authors.initials: PH
authors.lastname: Brown
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: Peter
authors.initials: P
authors.lastname: Schuck
mesh_terms: D000818:Animals; D001665:Binding Sites; D002021:Buffers; D006801:Humans; D007700:Kinetics; D008956:Models, Chemical; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D025941:Protein Interaction Mapping; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D013696:Temperature; D014461:Ultracentrifugation / Q000379:methods*
chemical_list: D002021:Buffers; D046912:Multiprotein Complexes; D011506:Proteins