The case for an empirical 'high-throughput' neutron scattering approach to protein dynamics

Recalling that there are currently more than 63,000 structures deposited in the Protein Data Bank, it is time for neutron scatterers studying protein dynamics to show a similar interest in the diversity that is the basis of biology. Sound experimental data that can underpin and complement molecular-dynamics simulations for fundamental research and health applications such as drug design can and should be provided. A proposal is presented to fulfil the two conditions that are required to enable such an approach: (i) the identification of measurable dynamics parameters that are correlated to biological function and activity and (ii) the design of experiments to measure these parameters efficiently with reasonable throughput.