Protein dynamics: hydration and cavities

Brazilian Journal of Medical and Biological Research

K. Heremans¹ 

[1] ,Katholieke Universiteit Leuven Departement of Chemistry Leuven,Belgium

关键词: Stability diagram;    Thermodynamics;    High pressure;    Unfolding;    Amyloid fibrils;    Protein dynamics;   

DOI  :  10.1590/S0100-879X2005000800002

来源: SciELO

【 摘 要 】

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.

【 授权许可】

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