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The effect of volume occupancy upon the thermodynamic activity of proteins: some biochemical consequences

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Summary

The thermodynamic activity of proteins in solution is substantially altered by the addition of unreactive or ‘inert’ macromolecules occupying more than a few percent of total solution volume. Approximate theoretical models of this effect have been formulated using a simplified geometrical representation of molecular shapes. These models predict that under certain conditions, the structure and function of proteins in physiological media with a high total macromolecular content may be qualitatively different than in dilute solution. Experimental studies of the effect of ‘inert’ macromolecules on protein structure and/or function are reviewed, and it is found that under favorable circumstances the simplified models can provide a satisfactory semiquantitative description of the data.

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Authors and Affiliations

  1. Laboratory of Biochemical Pharmacology, National Institute of Arthritis, Diabetes, and Digestive and Kidney Diseases, National Institutes of Health, Building 4, Room BI-27, 20205, Bethesda, MD, U.S.A.

    Allen P. Minton

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Minton, A.P. The effect of volume occupancy upon the thermodynamic activity of proteins: some biochemical consequences. Mol Cell Biochem 55, 119–140 (1983). https://doi.org/10.1007/BF00673707

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  • DOI: https://doi.org/10.1007/BF00673707

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