Human NAPE-PLD is a bile acid-dependent membrane enzyme that catalyzes the biogenesis of important bioactive lipid signaling molecules, which regulate immunity, energy balance, stress control and aging. Preliminary Neutron Scattering (NS) experiments at the IN13-backscattering in the temperature range 280 - 320 K have showed the overall protein dynamics is strongly affected by the presence of the bile acid deoxycholate (DC). With the present proposal we aim to conclude the preliminary results, and extend these studies on the dimer reorganization induced by DC, using the IN5 and IN13b beamlines. Both wild-type and a protein mutant that does not bind DC will be used for comparison as samples. NS measurements will be combined with other biophysical methodologies carried out at the Italian Institute of Technology, including FRET, EPR (NMR spin labelling), and in silico Molecular Dynamics.