Regensburg 2007 – scientific programme

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BP: Fachverband Biologische Physik

BP 26: Poster Session II

BP 26.22: Poster

Thursday, March 29, 2007, 17:00–19:30, Poster B

Simulation of transport through OmpF channels — •Soroosh Pezeshki, Mathias Winterhalter, and Ulrich Kleinekathöfer — International University Bremen (Jacobs University Bremen as of spring 2007), Campus Ring 1, 28759 Bremen, Germany

The outer membrane protein F (OmpF) trimer is a pore in the outer membrane of Escherichia coli. Since the crystal structure of OmpF is known, molecular dynamics simulations are possible [1,2]. Applying a constant electric field, the current caused by potassium and chlorine ions can be determined directly. Good agreement with experimental data is achieved [3]. In the constriction zone, i.e. the narrowest part of the pore, we additionally mutated charged amino acids to neutral ones. With the help of these mutated OmpF structures we investigated the influence of charged and neutral constriction zones on the ionic current. In a second step we are simulating the translocation of antibiotics molecules through the pore.

[1] K. M. Robertson and D. P. Tieleman, FEBS Lett. 528, 53 (2002).

[2] W. Im and B. Roux, J. Mol. Biol. 319, 1177 (2002).

[3] E. M. Nestorovich, C. Danelon, M. Winterhalter, and S. M. Bezrukov, PNAS 99, 9789 (2002).