Abstract
All biological activity critically depends on a correctly folded protein state, and folding takes place on the ribosome in an aqueous medium. Even in vitro, crystalline proteins contain almost 40% water (1). Hydration is therefore likely to play a major role in the maintenance of the native state. The physical properties of water, too, are sensitive to the same factors that influence protein stability, so that some connection is likely. Nevertheless, the realization that hydration might be an important factor in biological and technological function only dates from the early 1970s. Figure 1 summarizes the chronological development of our present understanding of two aspects of enzyme function: specificity and catalytic activity (2). It is now accepted that protein hydration interactions are of crucial importance in the maintenance of higher order structures and in rendering proteins useful as technological macromolecules. As will presently be shown, however, there is as yet little understanding about the details of such interactions and their role in determining the functional attributes of proteins.
Chronology of our understanding of the mechanisms that govern enzyme catalysis (ref. 2). Note that a consideration of solvation as a contributing factor dates only from 1970.
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Bibliography
Finney J. L. (1979) in Water—A Comprehensive Treatise, vol. 6 (Franks F., ed.) Plenum, New York, pp. 47–122.
Rupley J. A. (1979) in Characterisation of Protein Conformation and Function (Franks F., ed.) Symposium Press, London, pp. 54–61.
Franks F. (1975) in ref. 1, 4, 1–94.
Franks F. and Grigera J. R. (1990) Water Sci. Rev. 5, 187–289.
Friedman H. L. and Krishnan C.V. (1973) in ref. 1, 3, 1–118.
Enderby J. E. and Neilson G. W. (1979) in ref. 1, 6, 1–45.
Frank H. S. and Wen W. Y. (1957) Disc. Faraday Soc. 24, 133.
Conway B. E. (1981) Ionic Hydration in Chemistry and Biophysics, Elsevier, Amsterdam.
Friedman H. L. (1978) Faraday Disc. Chem. Soc. 64, 1.
Privalov P. L. and Khechinashvili N. N. (1974) J. Mol. Biol 86, 4291–4303.
Ratcliffe C. I. and Irish D. E. (1988) Water Sci. Rev. 3, 1–78.
Franks F. and Desnoyers J. E. (1985) Water Sci. Rev. 1, 171–232.
Davidson D. W. (1973) in ref. 1 115–234.
Eagland D. (1975) in ref. 1, 4, 305–518.
Franks F. and Eagland D. (1975) Crit. Rev. Biochem. 3, 165.
Pain R. H. (1979) in ref. 2, 19–36.
Finney J. L. (1982) in Biophysics of Water (Franks F. and Mathias S. F., eds.) John Wiley & Son, Chichester, pp. 55–57.
Chan D. Y., Mithcell D. J., Ninham B. W., and Pailthorpe B. A. (1979) in ref. 1, 6, 239–278.
Privalov P. L. and Gill S. J. (1989) Adv. Protein Chem. 39, 19–234.
Tanford C. (1973) The Hydrophobic Effect. John Wiley & Sons, New York.
Okazaki S., Nakanishi K., and Touhara H. (1983) J. Chem. Phys. 78, 454.
Dec S. F. and Gill S. J. (1985) J. Solution Chem. 14, 417.
Eisenberg D., Weiss R. M, Terwilliger T. C, and Wilcox W. (1982) Faraday Symp. Chem. Soc. 17, 109.
Nozaki Y. and Tanford C. (1971) J. Biol. Chem. 246, 2211.
Bigelow C. C. (1967) J. Theor. Biol. 16, 187.
Nord L., Tucker E. E., and Christian S. D. (1983) J. Solution Chem. 12, 889.
Franks F. and Pedley M. D. (1983) J. Chem. Soc. Faraday Trans I 79, 2249.
Lee B. and Richards F. M. (1971) J. Mol. Biol. 55, 379.
Shrake A. and Rupley J. A. (1973) J. Mol. Biol. 79, 351.
Savage H. F. J. (1986) Water Sci. Rev. 2, 67–148.
Drenth J., Jansonius J. N., Koekoek R., and Wolthers B. G. (1971) Adv. Protein Chem. 25, 79.
Berendsen H. J. C. (1975) in ref. 1, 5, 293–330.
Ramachandran G. N. and Chandrasekharan R. (1968) Biopolymers 6, 1649.
Chapman G. E., Danyluk S. S., and McLauchlan K. A. (1971) Proc. Roy. Soc. B 178, 465.
Birktoft J. J. and Blow D. M. (1972) J. Mol. Biol. 68, 187.
Vovelle F., Goodfellow J. M., Savage H. F. J., Barnes P., and Finney J. L. (1985) Eur. Biophys. J. 11, 225–237.
Teeter M. M. and Kossiakoff A. A. (1984) in Neutrons in Biology (Schoenborn B. P., ed.), Plenum, New York, p. 335.
Packer K. W. (1977) Phil. Trans. Roy. Soc. Ser. B. 278, 59–86.
Derbyshire W. (1982) in ref. 1, 7, 339–430.
Bryant R. G. and Halle B. (1982) in ref. 1 7, 389–393.
Kuntz I. D. and Kauzmann W. (1974) Adv. Protein Sci. 28, 239–255.
Cooke R. and Kuntz I. D. (1974) Ann. Rev. Biophys. Bioeng. 3, 95–126.
Clegg J. S. (1982) Mathias S. F., eds.) John Wiley & Son, Chichester in ref. 17, 365–383.
Ling G. N. and Negendank W. (1980) Persp. Biol. Med. 24, 215.
Privalov P. L. and Mrevlishvili G. M. (1967) Biofizika 12, 22.
Kuntz I. D. (1971) J. Amer. Chem. Soc. 93, 516.
McCabe V. C. and Fisher H. F. (1970) J. Phys. Chem. 74, 2990.
Pysh E. S. (1974) Biopolymers 13, 1557.
Franks F. (1991) Trends in Food Sci. Technol. 2, 68–72.
Ross H. K. (1954) Ind. Eng. Chem. 46, 601–610.
Rupley J. A., Gratton E., and Careri G. (1983) Trends Biochem. Sci. 8, 18–22.
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Franks, F. (1993). Protein Hydration. In: Franks, F. (eds) Protein Biotechnology. Biological Methods. Humana Press. https://doi.org/10.1007/978-1-59259-438-2_12
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DOI: https://doi.org/10.1007/978-1-59259-438-2_12
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