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Orientation and interactions of dipolar molecules during transport through OmpF porin
Author(s) -
Robertson Kindal M,
Tieleman D.Peter
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03173-3
Subject(s) - porin , periplasmic space , bacterial outer membrane , dipole , biophysics , molecule , membrane , chemistry , molecular dynamics , chemical physics , crystallography , escherichia coli , biology , biochemistry , computational chemistry , organic chemistry , gene
The outer membrane of Gram‐negative bacteria contains porins, large sieve‐like proteins allowing small molecules to diffuse in and out of the periplasm. We have simulated transport of the dipolar molecules alanine and methylglucose through the OmpF porin from Escherichia coli using non‐equilibrium steered molecular dynamics simulations in a realistic bilayer environment. Structural perturbation of the protein is minimal. During the permeation process, both alanine and methylglucose align strongly in the electric field in the eyelet region, where the adhesion force on the permeating molecule has a maximum. Binding of the permeating dipolar molecules in the eyelet region is not observed.