Abstract
Tertiary structures of proteins in aquaporin family have been investigated in detail about ten molecular species including glyceroporin, and the mechanism of substrate transportation based on the structures has been reported that the internal structure of the pore have an important role to transport substrate molecules. However, it is also important to understand the mechanism that there might be a regulation region on the surface of the protein. In this study, we examined in detail how molecular backborn structure would change with/without substrate. Since the tertiary structures of glyceroporin of E. coli. were obteined in different conditions with substrate, we took them from the database, and calculated to compare among them. As a result, existence of glycerol had little effect on the degree in slope of the transmembrane helices, but had a significant effect on the degree in twist and also the N-terminal structure of the sixth transmembrane helix.
