Membrane interactions control residues fluctuations of outer membrane porins

Bacterial outer membrane porins (Omp) that have robust ß-barrel structures, show potential ap-
plications for nanomedicine devices in synthetic membranes and single molecule detection biosensors.
Here, we explore the conformational dynamics of a set of 22 outer membrane porins, classified into
five major groups: general porins, specific porins, transport Omps, poreless Omps and composed
pores. Normal mode analysis, based on mechanical vibration theory and elastic network model, is
performed to study the fluctuations of residues of aforementioned porins around their equilibrium
positions. We find that a simple modification in this model considering weak interaction between
protein and membrane, dramatically enhance the stability of results and improve the correlation
coeficient between computational output and experimental results.

PHYSICAL REVIEW E 81, 051911 (2010)