Abstract
Changes in the conformation of a bovine rhodopsin, ich is a member of G-protein cowled receptor (GPCR) family, induced by external forces were simulated using a molecular dynamics simulation vith a computational software (NAMD 2.6, University of Illinois). Two molecular models were constructed; one is for a single thodopsin (modelR) and the other for the rhodopsin embedded into a lipid bilayer memlxane (model RM). The external forces were applied to the extracellular domain of the rhodopsin. As a result of simulation, the large conformation changes were exhibited near the extracellular domaiii In seven lransmemlxane α-helices the changes in both length and angle were the largest in the fourth α-helix, indicating that the fourth α-helix is the most affected by the external forces.
