Neutron scattering (NS) spectroscopy is a nondestructive technique that can be used to study the dynamics of protein in the liquid and solid states. It is sensitive to the position and motions of atoms and can probe spatial and temporal aspects of dynamics, which make it easier to determine what is being observed and the nature of the motion. The protein dynamic in the solid state can be easily impacted by external factors such as excipients, moisture/water content, and temperature. Several studies have connected high-frequency motions with the long-term stability of proteins. NS can be used to probe the protein dynamics in solid form and the principles and different types of neutron scattering have been extensively described in previous studies. This method involves monitoring the change in neutron scattering intensity by hydrogen atoms in the protein over time to observe protein dynamics. By measuring the mean-square displacements (MSD) (<u 2 >) of atoms within the protein molecule, the impact of external factors on protein dynamics can be evaluated. NS was extensively utilized to characterize the βfast dynamic process in dry proteins. This technique measures the <u 2 > of atoms in glasses, which represents the amplitude of fast motions on the nanosecond scale.