The goal of this project is to understand the antimicrobial activity of the intrinsically disordered salivary protein Histatin 5 (Hst5), which acts in defence against oral candidiasis caused by Candida albicans. Experiments and computer simulations have indicated the importance of the dynamic properties of the protein, and it is hypothesized the binding of ions, for example, Zn(+2) and Fe(+3), might be of importance. We aim to combine IN16B and IN5 to record the quasi-elastic neutron scattering spectra to cover a very complete dynamic range. The use of IN16B and IN15 in combination with novel data analysis frameworks to separate the different hierarchical levels of dynamics, it will allow for new insights that have not previously been accessible. The main goal will be to access the (sub) nanosecond internal diffusive motions of the proteins in solution, with emphasize on the parameters salt (zinc), protein concentration, and temperature. The model system, Hst5, is well established on both the experimental and simulation side, and by combining neutron scattering with simulations, we will obtain a molecular understanding of system that is both of medical and academic relevance.