Role of charged residues at the OmpF porin channel constriction probed by mutagenesis and simulation.

@article{Phale2001RoleOC,
  title={Role of charged residues at the OmpF porin channel constriction probed by mutagenesis and simulation.},
  author={Prashant S. Phale and Ansgar Philippsen and C L Widmer and V P Phale and J{\"u}rg P. Rosenbusch and Tilman Schirmer},
  journal={Biochemistry},
  year={2001},
  volume={40 21},
  pages={
          6319-25
        }
}
The channel constriction of OmpF porin, a pore protein in the bacterial outer membrane, is highly charged due to the presence of three arginines (R42, R82, and R132) and two acidic residues (D113 and E117). The influence of these charges on ion conductance, ion selectivity, and voltage gating has been studied with mutants D113N/E117Q, R42A/R82A/R132A/D113N/E117Q, and V18K/G131K, which were designed to remove or add protein charge at the channel constriction. The crystal structures revealed no… CONTINUE READING
Highly Cited
This paper has 53 citations. REVIEW CITATIONS

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 55 citations

53 Citations

0246'02'05'09'13'17
Citations per Year
Semantic Scholar estimates that this publication has 53 citations based on the available data.

See our FAQ for additional information.