Abstract :
The intrinsic energy of a (bio)molecule under study can be changed by chemical, thermal and mechanical perturbations. Most studies conducted in the fields of protein chemistry and biophysics make use of changing temperature (thermal perturbation) or adding denaturants (chemical perturbation) to the test tube - or combine both - to determine, e.g., changes in free energy, enthalpies or midpoints of conformational transitions.
Increasing hydrostatic pressure (mechanical perturbation) depicts another approach to obtain thermodynamic insights into the studied (bio)molecular system, especially when combined with high-resolution NMR spectroscopy. This presentation focuses on the application of high hydrostatic pressure NMR spectroscopy on proteins. Emphasis will be put on the precise determination of structural and dynamical parameters of the protein under study when hydrostatic pressure raises significantly above ambient conditions.