Importance of folded monomer and extended antiparallel dimer structures as enkephalin active conformation. Molecular dynamics simulations of [Met5]enkephalin in water.
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 beta-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 beta-bend monomer and the extended dimer structures exist together as the fundamental conformation of enkephalins.
Yoneda
S
S
Research Center, Taisho Pharmaceutical Co. Ltd, Saitama, Japan.
Kitamura
K
K
Doi
M
M
Inoue
M
M
Ishida
T
T
D002151:Calorimetry; D004744:Enkephalin, Methionine; D046911:Macromolecular Substances; D008958:Models, Molecular; D011487:Protein Conformation; D013314:Stress, Mechanical; D014867:Water
D046911:Macromolecular Substances; D014867:Water; D004744:Enkephalin, Methionine