title: Thermodynamic analysis of weak protein interactions using sedimentation equilibrium.
abstract: Proteins self-associate to form dimers and tetramers. Purified proteins are used to study the thermodynamics of protein interactions using the analytical ultracentrifuge. In this approach, monomer-dimer equilibrium constants are directly measured at various temperatures. Data analysis is used to derive thermodynamic parameters, such as Gibbs free energy, enthalpy, and entropy, which can predict which major forces are involved in protein association.
authors.affiliation: National Eye Institute, National Institutes of Health, Bethesda, Maryland.
authors.forename: Yuri V
authors.initials: YV
authors.lastname: Sergeev
authors.affiliation: National Eye Institute, National Institutes of Health, Bethesda, Maryland.
authors.forename: Monika B
authors.initials: MB
authors.lastname: Dolinska
authors.affiliation: National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland.
authors.forename: Paul T
authors.initials: PT
authors.lastname: Wingfield
mesh_terms: D019277:Entropy; D055503:Protein Multimerization; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D014461:Ultracentrifugation / Q000379:methods
chemical_list: D011506:Proteins
keywords: sedimentation equilibrium; thermodynamics; weak protein interaction
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