Thermodynamics of Protein-Protein Association

  • Philip D. Ross


This chapter is concerned with the thermodynamic parameters associated with protein-protein interactions. Protein-protein interactions may be classified either as homogeneous or heterogeneous, depending upon whether the polypeptide chains involved in association are the same or different. The former class are by definition polymerizations which may result in the formation of oligomers of definite structure and stoichiometry, aggregates composed of a distribution of molecular sizes, or large microtubular structures. Heterogeneous interactions include the association complexes formed between one protein and a different protein or protein fragment and also between nonidentical subunits of the same protein. The examples discussed below fall equally into these two classes.


Thermodynamic Parameter Entropy Change Enthalpy Change Gibbs Energy Change Heat Capacity Change 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



standard Gibbs energy change


standard enthalpy change


standard entropy change


standard molar heat capacity change All thermodynamic parameters are expressed per mole of complex formed except for the indefinite association cases of lysozyme, TMV protein and hemoglobin S for which the mole refers to the monomeric protein reacted. Standard states are hypothetical 1Mprotein and the pH at which the reaction was measured.


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© Springer-Verlag Berlin Heidelberg 1986

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  • Philip D. Ross

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