Protein dynamics: hydration and cavities.

K Heremans

doi:10.1590/s0100-879x2005000800002

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PubMed · 16082455

Protein dynamics: hydration and cavities.

K Heremans

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Abstract

The temperature-pressure behavior of proteins seems to be unique among the biological macromolecules. Thermodynamic as well as kinetic data show the typical elliptical stability diagram. This may be extended by assuming that the unfolded state gives rise to volume and enthalpy-driven liquid-liquid transitions. A molecular interpretation follows from the temperature and the pressure dependence of the hydration and cavities. We suggest that positron annihilation spectroscopy can provide additional quantitative evidence for the contributions of cavities to the dynamics of proteins. Only mature amyloid fibrils that form from unfolded proteins are very resistant to pressure treatment.

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Amyloid Hydrostatic Pressure Kinetics Models, Molecular Molecular Structure Protein Conformation Proteins Spectrum Analysis Thermodynamics Journal Article Review

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K Heremans. 2005-07-30. Protein dynamics: hydration and cavities.. https://doi.org/10.1590/s0100-879x2005000800002

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