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

Cite this

@article{de5f27550b924f2a860f08ef9ab8574f,
title = "The conformational preference of gramicidin channels is a function of lipid bilayer thickness.",
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.",
author = "Niloufar Mobashery and {Helix Nielsen}, Claus and Andersen, {Olaf S.}",
year = "1997",
language = "English",
volume = "421",
pages = "15--20",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd.",
number = "1",

}

The conformational preference of gramicidin channels is a function of lipid bilayer thickness. / Mobashery, Niloufar; Helix Nielsen, Claus; Andersen, Olaf S.

In: F E B S Letters, Vol. 421, No. 1, 1997, p. 15-20.

Research output: Contribution to journalJournal articleResearchpeer-review

TY - JOUR

T1 - The conformational preference of gramicidin channels is a function of lipid bilayer thickness.

AU - Mobashery, Niloufar

AU - Helix Nielsen, Claus

AU - Andersen, Olaf S.

PY - 1997

Y1 - 1997

N2 - 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.

AB - 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.

M3 - Journal article

VL - 421

SP - 15

EP - 20

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 1

ER -