Abstract
Biological macromolecules usually exhibit strong affinities for water. Protein crystals contain a considerable amount of bound water.1 The folded structure of a protein is known to be grossly altered if the bound water is completely removed from protein. Many globular proteins dissolved in the aqueous phase are found to be extensively hydrated.2 Fibrous proteins and other types of protein powders are known to adsorb a considerable amount of water vapor from the moist atmosphere forming protein gels. If the adsorption is extensive, many proteins may dissolve in the aqueous phase forming a concentrated solution. It may be pointed out here that the biological functions of protein such as enzyme activities, membrane transport, muscle action, water evaporation from skin, etc. are exhibited in the living system only in the presence of large amounts of aqueous fluid. It is believed that these functions are guided by complicated water-protein interactions, the mechanism of which is not yet clearly understood.
Keywords
- Surface Free Energy
- Free Energy Change
- Water Vapor Adsorption
- Isopiestic Equilibrium
- Water Vapor Adsorption Isotherm
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.
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© 1984 Plenum Press, New York
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Chattoraj, D.K., Birdi, K.S. (1984). Adsorption of Water Vapor by Biopolymers. In: Adsorption and the Gibbs Surface Excess. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-8333-2_9
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DOI: https://doi.org/10.1007/978-1-4615-8333-2_9
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