Some proteins within the body undergo some form of dynamics to perform their proper function. For example, proteins that metabolize certain ligands (small molecules such as metals or compounds) must "open" and "close" to bind and release the molecules during processing. These motions are of great interest to the scientific community, especially for drug design. These dynamical areas can be used as targets for personalized medicine in which drugs can be designed in such a way to utilize proteins with certain dynamical areas to metabolize the drug faster. In our lab we are developing an approach to identify and characterize protein dynamics using RDC data and the REDCRAFT software package. So far we have shown that our method is capable of identifying discrete motions of 30 degrees or greater in magnitude with high accuracy. As well as reconstructing the various states of dynamics, our method is also capable of estimating the relative occupancy of each state.
- Casey A. Cole, Rishi Mukhopadhyay, Hanin Omar, Mirko Hennig, and Homayoun Valafar. (2016). Structure Calculation and Reconstruction of Discrete-State Dynamics from Residual Dipolar Couplings. J. Chem. Theory Comput., 12 (4), pp 1408–1422. DOI: 10.1021/acs.jctc.5b01091