**3. "Global" Thermodynamic and Kinetic Parameters for Folding**/**Unfolding Reactions Obtained from 1D High-Pressure NMR Spectroscopy**

Typically, 1D HP-NMR can be used for steady-state measurements, recorded when the ratio between folded/unfolded protein populations has reached equilibrium after a pressure jump. Such measurements give access to the global thermodynamic parameters ∆*G* 0 (the free-energy difference at atmospheric pressure between the folded and unfolded states of the protein) and ∆*V* 0 (the volume difference at atmospheric pressure between the folded and unfolded states of the protein), characteristic of the folding/unfolding reaction. In addition, kinetic measurements recorded just after the *P*-jump, while establishing equilibrium, are also possible with HP-NMR, yielding kinetic information on the folding/unfolding reaction as well as volumetric properties of protein folding transition states.
