Protein Dynamics under Non-Ambient Conditions
Protein flexibility plays a central role in enzymatic activities, their regulation, the binding of native ligands and drugs and other biomolecular processes. Therefore, the study of protein dynamics is a prerequisite for understanding these mechanisms. A temperature-jump method was developed to obtain time-resolved X-ray crystal structures and thus to analyse proteins in motion. The experimental data obtained can be compared with in silico methods, such as molecular dynamics simulations, to subsequently analyse the effects of various perturbations on protein behaviour, enable predictions of protein dynamics and create generic models of protein flexibility.