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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

The Temperature Dependence of Gramicidin Conformational States in Octanol

Author(s): Farah O'Boyle and B. A. Wallace

Volume 10, Issue 1, 2003

Page: [9 - 17] Pages: 9

DOI: 10.2174/0929866033408246

Price: $65

Abstract

In lipid bilayers and organic solvents, the hydrophobic polypeptide gramicidin adopts a number of different conformations, some of which are capable of conducting monovalent cations across phospholipid membranes. The equilibria between conformations have been shown to be influenced by factors such as lipid chain length, solvent, concentration and salt. In this study, the temperature dependence of the equilibrium mixture of double helical ion-free gramicidin in octanol was examined using circular dichroism spectroscopy.

Keywords: gramicidin, octanol, hydrophobic polypeptide


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