Abstract
High hydrostatic pressure has been used as a physical parameter for studying the stability of biomolecular systems, such as lipid bilayers, DNA and proteins, but also because high pressure is an important feature of certain natural environments. By using a variety of spectroscopic, calorimetric and scattering techniques, the temperature and pressure dependent structure and phase behavior of these systems has been studied and will be discussed. We also introduce pressure as a kinetic variable. Applying the pressure-jump relaxation technique in combination with time-resolved synchrotron X-ray diffraction and spectroscopic techniques, the kinetics of lipid phase transitions and folding reactions of proteins has been studied. Finally, recent advances in using pressure for studying misfolding and aggregation of proteins will be elucidated.
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