| Literature DB >> 25081741 |
Yuri V Sergeev1, Monika B Dolinska1, Paul T Wingfield2.
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.Entities:
Keywords: sedimentation equilibrium; thermodynamics; weak protein interaction
Mesh:
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Year: 2014 PMID: 25081741 PMCID: PMC4182932 DOI: 10.1002/0471140864.ps2013s77
Source DB: PubMed Journal: Curr Protoc Protein Sci ISSN: 1934-3655