The influence of amino acid protonation states on molecular dynamics simulations of the bacterial porin OmpF.

Abstract excerpt

Several groups, including our own, have found molecular dynamics (MD) calculations to result in the size of the pore of an outer membrane bacterial porin, OmpF, to be reduced relative to its size in the x-ray crystal structure. At the narrowest portion of its pore, loop L3 was found to move toward the opposite face of the pore, resulting in decreasing the cross-section area by a factor of approximately 2. In an...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Hydrogen Bonding
• Share to Ions
• Share to Lipid Bilayers