Abstract
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.
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Abbreviations
- ∆G0 :
-
standard Gibbs energy change
- ∆H0 :
-
standard enthalpy change
- ∆S0 :
-
standard entropy change
- ∆C 0p :
-
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.
References
Hearn RP, Richards FM, Sturtevant JM, Watt GD (1971) Biochemistry 10: 806–817
Yung HYK, Trowbridge CG (1980) J Biol Chem 255: 9724–9730
Lavialle F, Rogard M, Alfsen A (1974) Biochemistry 13: 2231–2234
Wiesinger H, Bartholmes P, Hinz H-J (1979) Biochemistry 18: 1979–1984
Johnson RE, Hruby VJ, Rupley JA (1979) Biochemistry 18: 1176–1179
Banerjee SK, Pogolotti A Jr, Rupley JA (1975) J Biol Chem 250: 826–8266
Shiao DF, Sturtevant JM (1969) Biochemistry 8: 4910–4917
Atha DH, Ackers GK (1974) Arch Biochem Biophys 164: 392–407
Sturtevant JM, Velicelebi G, Jaenicke R, Lauffer MA (1981) Biochemistry 20: 3792–3800
Ross PD, Hofrichter J, Eaton WA (1977) J Mol Biol 115: 111–134
Gill SJ, Farquhar EL (1968) J Am Chem Soc 90: 3039–3041
Turner R, Liener IE, Lovrien RE (1975) Biochemistry 14: 275–282
Ross PD, Hofrichter J, Eaton WA (1975) J Mol Biol 96: 239–256
Ross PD, Minton AP (1977) J Mol Biol 112: 437–452
Ross PD, Subramanian S (1981) Biochemistry 20: 3096–3102
Chen CH, Berns DF (1977) J Phys Chem 81: 125–129
Hinz H-J (1983) Ann Rev Biophys Bioeng 12: 285–317
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© 1986 Springer-Verlag Berlin Heidelberg
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Ross, P.D. (1986). Thermodynamics of Protein-Protein Association. In: Hinz, HJ. (eds) Thermodynamic Data for Biochemistry and Biotechnology. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71114-5_8
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DOI: https://doi.org/10.1007/978-3-642-71114-5_8
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