In this work results of neutron powder diffraction and inelastic neutron scattering on aliphatic amino acid (L-alanine, L-valine and L-leucine) crystals are presented. The study allows inferring important informations about both the stability of the structures and the dynamics of phase transitions. In particular, it was possible to compare the behavior of different amino acids and to infer that changes in the mean-square displacements observed for two deuterated forms of L-alanine ND3+ – C2H4 – CO2- and NH3+ – C2D4 – CO2- are due to a structural rearrangement related to thermally activated amplitude reorientation of NH3+ and CO2-. Conformation changes in L-valine and L-leucine related to the phase transition are also discussed
