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Biophysical studies of membrane proteins/peptides. Interaction with ...

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acceptors) (Eqs. 4-6) (⋅-⋅-⋅). A: A model assuming binding <strong>of</strong> cipr<strong>of</strong>loxacin near the<br />

trimer interface (Model I) was fitted to the experimental data (Eqs. 4-12). The interval<br />

<strong>of</strong> 3.15 < log(K B ) < 3.62 was recovered for the binding constant (grey area). B: A model<br />

assuming binding <strong>of</strong> cipr<strong>of</strong>loxacin to the OmpF periphery (Model II) was fitted to the<br />

experimental data. The interval <strong>of</strong> 3.58 < log(K B ) < 4.00 was recovered for the binding<br />

constant (grey area). The simulations for the upper and lower bounds <strong>of</strong> K B are<br />

represented in both figures by a solid line (⎯) and by a dotted line (⋅⋅⋅⋅⋅), respectively.<br />

Figure A1 – Schematic side (A) and top (B) views <strong>of</strong> a lipid bilayer containing a<br />

cylindrical <strong>membrane</strong> protein labelled <strong>with</strong> a donor fluorophore (D) at its outer radius,<br />

capable <strong>of</strong> FRET to acceptors (A) located in the lipid bilayer, on a plane parallel to the<br />

bilayer plane. See text for details.<br />

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