Editorial Functional Dynamics of Proteins

Copyright © 2012 Lee-Wei Yang et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. X-ray crystallography captures protein conformational states that are stable enough to be captured. These observable states are simply part of the functional event in the context of protein dynamics. Life at the molecular level has a vibrant nature at physiological temperature, governed by physics laws. Molecular dynamics (MDs) simulations have been used to study biomolecular systems since 1970s [1]. Advancing to this day, it has been a common practice for researchers who access supercomputers to obtain trajectories for hundreds of nanoseconds to two microseconds for small proteins [2, 3] and a few tens of nanoseconds for supramolecular assemblies such as the ribosome of a size larger than 200 A