Abstract
In Chapter 4 the marginal stability of native proteins was discussed with reference to the effects of environmental factors such as temperature, pressure, and additives. It must also be stressed that biological activity critically depends on a correctly folded 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.
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Franks, F. (1988). Protein Hydration. In: Franks, F. (eds) Characterization of Proteins. Biological Methods. Humana Press. https://doi.org/10.1007/978-1-59259-437-5_5
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DOI: https://doi.org/10.1007/978-1-59259-437-5_5
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