title: Molecular dynamics study of aquaporin-1 water channel in a lipid bilayer.
abstract: The aquaporin-1 water channel was modeled in a palmitoyl-oleoyl-phosphatidyl-choline lipid bilayer, by means of molecular dynamics simulations. Interaction of the protein with the membrane and inter-monomer interactions were analyzed. Structural features of the channel important for its biological function, including the Asn-Pro-Ala (NPA) motifs, and the diffusion of water molecules into the channels, were investigated. Simulations revealed the formation of single file water inside the channels for certain relative positions of the NPA motifs.
authors.affiliation: Beckman Institute, University of Illinois at Urbana-Champaign, 405 N. Mathews, Urbana, IL 61801, USA.
authors.forename: F
authors.initials: F
authors.lastname: Zhu
authors.forename: E
authors.initials: E
authors.lastname: Tajkhorshid
authors.forename: K
authors.initials: K
authors.lastname: Schulten
mesh_terms: D051398:Aquaporin 1; D020346:Aquaporins / Q000737:chemistry* / Q000378:metabolism*; D001789:Blood Group Antigens; D016208:Databases, Factual; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry*; D050356:Lipid Metabolism; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013997:Time Factors; D014867:Water / Q000737:chemistry*
chemical_list: C496020:AQP1 protein, human; D020346:Aquaporins; D001789:Blood Group Antigens; D008051:Lipid Bilayers; D014867:Water; D051398:Aquaporin 1