The conformational preference of gramicidin channels is a function of lipid bilayer thickness Academic Article Article uri icon

Overview

MeSH Major

  • Gramicidin
  • Lipid Bilayers
  • Membrane Transport Proteins

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.

publication date

  • July 21, 1997

Research

keywords

  • Academic Article

Identity

Digital Object Identifier (DOI)

  • 10.1016/S0014-5793(97)00709-6

PubMed ID

  • 9257681

Additional Document Info

start page

  • 15

end page

  • 20

volume

  • 412

number

  • 1