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High Pressure Molecular Science pp 437–472Cite as

The Phase Diagram and the Pressure-Temperature Behavior of Proteins

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Part of the book series: NATO Science Series ((NSSE,volume 358))

Abstract

The pressure and temperature behavior of proteins is discussed in the framework of the phase diagram. This gives unique information on the changes in heat capacity, thermal expansion and compressibility of protein unfolding. It also relates the cold, heat and pressure denaturation. The difference in pressure- and temperature-induced aggregation of unfolded proteins shows the unique features of pressure effects. A molecular interpretation of the thermodynamic quantities is not possible on the basis of model systems unless the packing defects are taken into account. High pressure molecular dynamic calculations contribute in a unique way to our understanding of pressure effects.

A fresh instrument serves the same purpose as foreign travel; it shows things in unusual combinations. A. N. Whitehead in: Science and modern world.

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Authors and Affiliations

  1. Department of Chemistry, Katholieke Universiteit Leuven, B-3001, Leuven, Belgium

    Karel Heremans

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  1. Karel Heremans
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  1. Department of Chemistry, Physical Chemistry, University of Dortmund, Dortmund, Germany

    Roland Winter

  2. School of Chemical Sciences, University of Illinois, Urbana, Illinois, USA

    Jiri Jonas

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Heremans, K. (1999). The Phase Diagram and the Pressure-Temperature Behavior of Proteins. In: Winter, R., Jonas, J. (eds) High Pressure Molecular Science. NATO Science Series, vol 358. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4669-2_23

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  • DOI: https://doi.org/10.1007/978-94-011-4669-2_23

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