In recent years, there has been increasing interest in exploiting the effects of applied pressure on biological systems because recent progress were observed in basic science due both to elaboration of new concepts and to technological improvements. For example, major biophysical methods have been adapted to HP conditions.
In our laboratory, methods to study fast kinetics reactions under HP have been developed using, as detection, absorbency or fluorescence spectroscopies. It is the stopped-flow method allowing the determination of activation volume of the reaction under study.
To approach protein conformation and protein flexibility, two ways are actually very easily used: the fourth UV-visible spectroscopy and the fluorescence spectroscopy. For both, the aromatic amoniacid compounds (tryptophan, tyrosine and phenylalanine) can be used as internal probes. Another external fluorescence probe can be also used (ANS) to explore the hydrophobic core of the proteins.
Recently, in the laboratory, different experiments were achieved using these methods, and the results will be presented and discussed, together with some putative biotechnological applications.
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