Covalently linked gramicidin channels: Effects of linker hydrophobicity and alkaline metals on different stereoisomers

Biophysical Journal

Volumn 80, Issue 4, 2001, Pages 1810-1818

  Armstrong, Kathryn M ^a   Quigley, Edward P ^a   Quigley, Paulene ^b   Crumrine, David S ^b   Cukierman, Samuel ^a  

^a LOYOLA UNIVERSITY CHICAGO   (United States)

^b LOYOLA UNIVERSITY CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALKALI METAL; CESIUM ION; GRAMICIDIN; GRAMICIDIN A; ION CHANNEL; POTASSIUM ION;

ARTICLE; CHANNEL GATING; COVALENT BOND; HYDROPHOBICITY; LIPID BILAYER; LIPID MEMBRANE; MOLECULAR DYNAMICS;

EID: 0035073446     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(01)76151-6     Document Type: Article

References (5)

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2. Arseniev, A. S., I. L. Barsukov, V. F. Bystrov, A. L. Lonize, and Y. A. Ovchinikov. 1985. Proton NMR study of gramicidin A transmembrane ion channel. Head-to-head right handed, single stranded helices. FEBS Lett. 186:168-174.
3. Bamberg, E., and K. Janko. 1977. The action of a carbonsuboxide dimerized gramicidin A on lipid bilayer membranes. Biochem. Biophys. Acta. 465:486-499.
4. Burkhart, B. M., and W. L. Duax. 1999. Gramicidin channel controversy: reply. Nat. Struct. Biol. 6:611-612.
5. Burkhart, B. M., N. Li, D. A. Langs, W. A. Pangborn, and W. L. Duax. 1998. The conducting form of gramicidin A is a right-handed double-stranded double helix. Proc. Natl. Acad. Sci. U.S.A. 95:12950-12955.