The conformational preference of gramicidin channels is a function of lipid bilayer thickness.

Niloufar Mobashery, Claus Helix Nielsen, Olaf S. Andersen

Research output: Contribution to journalJournal articleResearchpeer-review

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 languageEnglish
JournalF E B S Letters
Volume421
Issue number1
Pages (from-to)15-20
ISSN0014-5793
Publication statusPublished - 1997
Externally publishedYes

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