Importance of folded monomer and extended antiparallel dimer structures as enkephalin active conformation Molecular dynamics simulations of [Met5]enkephalin in water

Abstract
Simulations of the molecular dynamics of the [Met5]enkephalin monomer and dimer structures in water have been carried out. The dynamic trajectories have been analyzed in terms of the distances between intra‐ or intermolecular polar atoms. The time‐correlated conformational transitions of an extended monomer structure have been converged into a stationary state among the β‐bend folded forms. However, the dynamics simulation of an extended antiparallel dimer structure has shown no noticeable conformation change. These results imply that both the β‐bend monomer and the extended dimer structures exist together as the fundamental conformation of enkephalins.