Channels formed by colicin E1 in planar lipid bilayers are large and exhibit pH-dependent ion selectivity
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Physiology,Biophysics
Link
http://link.springer.com/content/pdf/10.1007/BF01872215.pdf
Reference16 articles.
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2. Cramer, W.A., Dankert, J.R., Uratani, Y. 1983. The membrane channel-forming bacteriocidal protein, colicin E1.Biochim. Biophys. Acta 737:173–193
3. Dwyer, T.M., Adams, D.J., Hille, B. 1980. The permeability of the endplate channel to organic cations in frog muscle.J. Gen. Physiol. 75:469–492
4. Greenfield, L., Bjorn, M., Horn, G., Fong, D., Buck, G., Collier, J., Kaplan, D. 1983. Nucleotide sequence of the structural gene for diphtheria toxin carried by corynebacteriophage.Proc. Natl. Acad. Sci. USA 80:6853–6857
5. Heyer, E., Muller, R., Finkelstein, A. 1976. Inactivation of monazomycin-induced voltage-dependent conductance in thin lipid membranes. II. Inactivation produced by monazomycin transport through the membrane.J. Gen. Physiol. 67:731–748
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