Abstract
The methods of study of proteins under high pressure, and the effects of pressure upon proteins made up of a single peptide chain are briefly reviewed. The effects upon oligomeric proteins are examined in detail: The existence of time-dependent changes in the conformation of the dissociated subunits, termed a “conformational drift”, is revealed by the temporary decreases in subunit affinity, enzymic activity and changed spectroscopic properties of the aggregates formed after decompression. Its significance in relation to the equilibria established under pressure is discussed and the insuficiency of conventional descriptions of the chemical equilibrium for these cases is noted.
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© 1987 D. Reidel Publishing Company
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Weber, G. (1987). Dissociation of Oligomeric Proteins by Hydrostatic Pressure. In: van Eldik, R., Jonas, J. (eds) High Pressure Chemistry and Biochemistry. NATO ASI Series, vol 197. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-3827-4_17
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DOI: https://doi.org/10.1007/978-94-009-3827-4_17
Publisher Name: Springer, Dordrecht
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