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

FEBS Letters

Doi, Mitsunobu¹  Yoneda, Shigetaka²  Inoue, Masatoshi¹  Ishida, Toshimasa¹  Kitamura, Kunihiro² 

[1]Osaka University of Pharmaceutical Sciences, 2-10-65 Kawai, Matsubara, Osaka 580, Japan

[2]Research Center, Taisho Pharmaceutical Co. Ltd, 1-403 Yoshino-cho, Ohmiya, Saitama 330, Japan

关键词: Enkephalin;    Molecular dynamics simulation;    β-Bend conformation;    Extended antiparallel dimer conformation;   

DOI  :  10.1016/0014-5793(88)80932-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown