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Thermodynamics of Protein-Protein Association

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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

  1. Hearn RP, Richards FM, Sturtevant JM, Watt GD (1971) Biochemistry 10: 806–817

    Article  CAS  Google Scholar 

  2. Yung HYK, Trowbridge CG (1980) J Biol Chem 255: 9724–9730

    Article  CAS  Google Scholar 

  3. Lavialle F, Rogard M, Alfsen A (1974) Biochemistry 13: 2231–2234

    Article  CAS  Google Scholar 

  4. Wiesinger H, Bartholmes P, Hinz H-J (1979) Biochemistry 18: 1979–1984

    Article  CAS  Google Scholar 

  5. Johnson RE, Hruby VJ, Rupley JA (1979) Biochemistry 18: 1176–1179

    Article  CAS  Google Scholar 

  6. Banerjee SK, Pogolotti A Jr, Rupley JA (1975) J Biol Chem 250: 826–8266

    Article  Google Scholar 

  7. Shiao DF, Sturtevant JM (1969) Biochemistry 8: 4910–4917

    Article  CAS  Google Scholar 

  8. Atha DH, Ackers GK (1974) Arch Biochem Biophys 164: 392–407

    Article  CAS  Google Scholar 

  9. Sturtevant JM, Velicelebi G, Jaenicke R, Lauffer MA (1981) Biochemistry 20: 3792–3800

    Article  CAS  Google Scholar 

  10. Ross PD, Hofrichter J, Eaton WA (1977) J Mol Biol 115: 111–134

    Article  CAS  Google Scholar 

  11. Gill SJ, Farquhar EL (1968) J Am Chem Soc 90: 3039–3041

    Article  CAS  Google Scholar 

  12. Turner R, Liener IE, Lovrien RE (1975) Biochemistry 14: 275–282

    Article  CAS  Google Scholar 

  13. Ross PD, Hofrichter J, Eaton WA (1975) J Mol Biol 96: 239–256

    Article  CAS  Google Scholar 

  14. Ross PD, Minton AP (1977) J Mol Biol 112: 437–452

    Article  CAS  Google Scholar 

  15. Ross PD, Subramanian S (1981) Biochemistry 20: 3096–3102

    Article  CAS  Google Scholar 

  16. Chen CH, Berns DF (1977) J Phys Chem 81: 125–129

    Article  CAS  Google Scholar 

  17. Hinz H-J (1983) Ann Rev Biophys Bioeng 12: 285–317

    Article  CAS  Google Scholar 

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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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  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-71116-9

  • Online ISBN: 978-3-642-71114-5

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