Genetically Engineered Metal Ion Binding Sites on the Outside of a Channel's Transmembrane Β-Barrel

Published

February 1, 1999

Author(s)

John J. Kasianowicz, D L. Burden, L C. Han, S Cheley, H Bayley

Abstract

We are exploring the ability of genetically engineered versions of the Staphlococcus aureus αHL} ion channel to serve as rationally designed sensor components for analytes including divalent cations. We show here that neither the hemolytic activity nor the single channel current of wild type αHL were affected by [Zn(II)]

Citation

Biophysical Journal

Volume

76

Issue

2

Pub Type

Journals

Keywords

alpha-hemolysin, alpha-toxin, biosensor, divalent cations, ion channels, protein structure, transition metals

Citation

Kasianowicz, J. , Burden, D. , Han, L. , Cheley, S. and Bayley, H. (1999), Genetically Engineered Metal Ion Binding Sites on the Outside of a Channel's Transmembrane Β-Barrel, Biophysical Journal (Accessed April 20, 2024)