The conformational preference of gramicidin channels is a function of lipid bilayer thickness1This work has already appeared in abstract form: C. Nielsen, Mobashery, N. and Andersen, O.S., Biophys. J., 72:A191.1

In order to understand how the material properties of lipid bilayers could affect integral membrane protein function, we examined the effect of a hydrophobic mismatch on the structure and function of membrane-spanning gramicidin channels. Changes in lipid bilayer thickness affect the conformational preference of membrane-spanning gramicidin A (gA) channels (single–stranded [SS] dimers ↔ double-stranded [DS] dimers) and induces an additional conductance state in the standard (SS) β6.3-helical channel. These results provide experimental evidence for the importance of energetic coupling between the bilayer and imbedded inclusions.