Electron paramagnetic resonance spectroscopy is used to characterize the active site dynamics of alpha-chymotrypsin solubilized in reversed micelles. Of particular interest is the behavior of the enzyme when the micellar system is subjected to enhanced gas pressures and low temperatures. At specific thermodynamic conditions, clathrate hydrates form from the intramicellar water, reducing the micelle size and water content. Also, beyond a critical pressure, micellar instability results. The EPR spectra under these conditions indicate that the rotational correlation times increase appreciably only when the water-to-surfactant molar ratio, w0, is reduced to values lower than 10. The EPR characterization also reveals a remarkable resilience of the enzyme when subjected to pressure-induced changes; when returned to ambient conditions, activity and active site dynamics are fully restored.