Association and Folding of Small Oligomeric Proteins

AbstractOriginally published in: Protein Folding Handbook. Part I. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2The sections in this article areIntroductionExperimental Methods Used to Follow the Folding of Oligomeric ProteinsEquilibrium MethodsKinetic MethodsDimeric ProteinsTwo‐state Folding of Dimeric ProteinsExamples of Dimeric Proteins Obeying Two‐state FoldingFolding of Dimeric Proteins through Intermediate StatesTrimeric and Tetrameric ProteinsConclusionsAppendix–Concurrent Association and Folding of Small Oligomeric ProteinsEquilibrium Constants for Two‐state FoldingHomooligomeric ProteinHeterooligomeric ProteinCalculation of Thermodynamic Parameters from Equilibrium ConstantsBasic Thermodynamic RelationshipsLinear Extrapolation of Denaturant Unfolding Curves of Two‐state ReactionCalculation of the van't Hoff Enthalpy Change from Thermal Unfolding DataCalculation of the van't Hoff Enthalpy Change from the Concentration‐dependence ofTmExtrapolation of Thermodynamic Parameters to Different Temperatures:Gibbs‐Helmholtz EquationKinetics of Reversible Two‐state Folding and Unfolding: Integrated Rate EquationsTwo‐state Folding of Dimeric ProteinTwo‐state Unfolding of Dimeric ProteinReversible Two‐state Folding and UnfoldingHomodimeric proteinHeterodimeric proteinKinetics of Reversible Two‐state Folding: Relaxation after Disturbance of a Preexisting Equilibrium (Method ofBernasconi)Acknowledgments