Open AccessThermodynamic Analysis of Weak Protein Interactions Using Sedimentation Equilibrium
Author(s) -
Sergeev Yuri V.,
Dolinska Monika B.,
Wingfield Paul T.
Publication year - 2014
Publication title -
current protocols in protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.409
H-Index - 32
eISSN - 1934-3663
pISSN - 1934-3655
DOI - 10.1002/0471140864.ps2013s77
Subject(s) - sedimentation equilibrium , chemistry , thermodynamics , biophysics , statistical physics , physics , biology , chromatography , ultracentrifuge
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. Curr. Protoc. Protein Sci . 77:20.13.1‐20.13.15. © 2014 by John Wiley & Sons, Inc.