Probing the dynamics of biological matter by elastic, quasi-elastic, and inelastic neutron scattering

The so-called function-structure-dynamics paradigm established that a close relationship links the way biological molecules work (function), their 3-dimensional organization (structure) and the changes of this organization in time (dynamics), which characterize biomolecules as highly dynamic objects. A typical example of protein dynamics is provided by protein reactions with substrates: equilibrium thermal fluctuations of protein structure are necessary to allow the access of substrates to the active site, where the functional reaction occurs. Neutron scattering is a powerful technique to study equilibrium protein structural dynamics. The incoherent structure factor, which is dominant in neutron scattering from biological matter, is related to the time-position self correlation function of protein/solvent nuclei. Here the basic theory of neutron scattering and the principles of the technologies used to measure it are described. Some selected applications of neutron scattering for investigating the structural dynamics of biological molecules are also reviewed.