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) beta6.3-helical channel. These results provide experimental evidence for the importance of energetic coupling between the bilayer and imbedded inclusions.
|Journal||F E B S Letters|
|Publication status||Published - 1997|