Abstract
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.
| Original language | English |
|---|---|
| Journal | F E B S Letters |
| Volume | 421 |
| Issue number | 1 |
| Pages (from-to) | 15-20 |
| ISSN | 0014-5793 |
| Publication status | Published - 1997 |
| Externally published | Yes |