Structural dynamics and computational design of synthetic enzymes

Natural enzymes can adopt many conformations, widening each state within their rugged energy landscape. This structural flexibility allows for entropic as well as enthalpic reaction rate accelerations. Computational methods, at the forefront of enzyme-related research, are developed to understand enzymatic mechanisms from the ground up. These fundamental principles can then be translated into rational design protocols for synthetic enzymes. Thus far, our design strategies have revolved around the optimization of a single protein conformation. They must be then updated to reflect our current knowledge of a more dynamic picture of enzymatic catalysis.