A synergistic approach is described combining computer simulation with experiment in the interpretation of small angle neutron scattering (SANS) and inelastic scattering experiments on the structure and dynamics of proteins and other biopolymers. Simulation models can be tested by calculating neutron scattering structure factors and comparing the results directly with experimental scattering profiles. If the scattering profiles agree the simulations can be used to provide a detailed decomposition and interpretation of the experiments, and if not, the models can be rationally adjusted. Comparison with neutron experiment can be made at the level of the scattering functions or, less directly, of structural and dynamical quantities derived from them. This methodology is discussed in the context of the protein glass transition, protein-solvent dynamical coupling, the density of the hydration shell of proteins and the structural analysis of lignocellulosic biomass.