Dynamics of water molecules in the bacteriorhodopsin trimer in explicit lipid/water environment.

ABSTRACT: Protonated networks of internal water molecules appear to be involved in proton transfer in various integral membrane proteins. High-resolution x-ray studies of protein crystals at low temperature deliver mean positions of most internal waters, but only limited information about fluctuations within such H-bonded networks formed by water and residues. The question arises as to how water molecules behave inside and on the surface of a fluctuating membrane protein under more physiological conditions. Therefore, as an example, long-time molecular dynamics simulations of bacteriorhodopsin were performed with explicit membrane/water environment. Based on a recent x-ray model the bacteriorhodopsin trimer was inserted in a fully solvated 16 x 16 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (PO

SUBMITTER: Kandt C 

PROVIDER: S-EPMC1303921 | biostudies-literature | 2004 Feb

REPOSITORIES: biostudies-literature