The Temperature Dependence of Gramicidin Conformational States in Octanol

Farah      O'Boyle; B.   A.   Wallace

doi:10.2174/0929866033408246

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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Protein & Peptide Letters

Title: The Temperature Dependence of Gramicidin Conformational States in Octanol

Volume: 10 Issue: 1

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

Affiliation:

Keywords: gramicidin, octanol, hydrophobic polypeptide

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.

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Cite this article as:

O'Boyle Farah and Wallace A. B., The Temperature Dependence of Gramicidin Conformational States in Octanol, Protein & Peptide Letters 2003; 10 (1) . https://dx.doi.org/10.2174/0929866033408246

DOI https://dx.doi.org/10.2174/0929866033408246	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305

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