Probing the dynamics of a protein hydrophobic core by deuteron solid-state nuclear-magnetic resonance spectroscopy

Deuteron NMR quadrupolar echo line shape analysis are used for examining dynamical features of hydrophobic cores of proteins over a wide range of temperatures. Relaxation behavior is described by a phenomenological distribution of activation energies for three-site hops at high temperatures that collapses to a single, distinctly smaller value for lower temperatures.