FEBS Letters
Volume 412, Issue 1 , Pages 15-20, 21 July 1997

The conformational preference of gramicidin channels is a function of lipid bilayer thickness 1

Department of Physiology and Biophysics, Cornell University Medical College, 1300 York Avenue, New York, NY 10021, USA

Received 19 May 1997

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) β6.3-helical channel. These results provide experimental evidence for the importance of energetic coupling between the bilayer and imbedded inclusions.

Keywords:  Hydrophobic matching , Membrane deformation energy , Single stranded channel , Double stranded channel

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  • 1 This work has already appeared in abstract form: C. Nielsen, Mobashery, N. and Andersen, O.S., Biophys. J., 72:A191.

PII: S0014-5793(97)00709-6

doi:10.1016/S0014-5793(97)00709-6

FEBS Letters
Volume 412, Issue 1 , Pages 15-20, 21 July 1997

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