Neutron scattering perspectives for protein dynamics

After a double decade of intensive neutron scattering studies of the biological physics of protein dynamics on a few well-characterised model systems, the time has come to extend the method to address the vast biological diversity of proteins and their dynamics-function relationships. The time-scale and length-scale dependent mean square displacement and effective force constant, measured by neutron elastic intensity temperature scans, are proposed as relevant experimental parameters, and examples are given of their correlation with biological function. The parameters are directly calculable from molecular dynamics simulations, and their proposed deposit in an accessible data bank will greatly strengthen the links between experimental and theoretical approaches to protein dynamics.