Study of the conformational changes in Intrinsically disordered proteins through MD simulation.
Proteins acquire different conformations which determine their structure and function. Several of the pore forming proteins investigated in our group undergo large conformational changes such as beta sheets to alpha helices or vice-versa upon contact with the lipid membrane. In several cases disordered regions of protein play a central role in its functioning. The role of these disordered regions is poorly understood. In other cases, the protein is intrinsically disordered without any specific resolved crystal structure and manner in which these proteins functions is an active area of research. Disordered proteins are responsible for a wide range of biological functions in an organism. Our aim is to formulate the landscape sampled by disordered proteins by creating an energy landscape through free energy calculations which can be useful for functioning of disordered regions in proteins.