Ion interactions in (1-13C)d-Val8 andd-Leu14 analogs of gramicidin A, the helix sense of the channel and location of ion binding sites
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Physiology,Biophysics
Link
http://link.springer.com/content/pdf/10.1007/BF01870401.pdf
Reference39 articles.
1. Apell, H.-J., Bamberg, E., Alpes, H., Läuger, P. 1977. Formation of ion channels by a negatively charged analog of gramicidin A.J. Membrane Biol. 31:171–188
2. Bamberg, E., Apell, H.-J., Alpes, H. 1977. Structure of the gramicidin A channel: Discrimination between theL,D, and the helix by electrical measurements with lipid bilayer membranes.Proc. Natl. Acad. Sci. USA 74:2402–2406
3. Bamberg, E., Apell, H.J., Bradley, R., Härter, B., Quelle, M.-J., Urry, D.W. 1979. Formation of ionic channels in black lipid membranes by succinic derivatives of gramicidin A.J. Membrane Biol. 50:257–270
4. Bamberg, E., Janko, K. 1977. The action of a carbonsuboxide dimerized gramicidin A on lipid bilayer membranes.Biochim. Biophys. Acta. 465:486–499
5. Bamberg, E., Läuger, P. 1977. Blocking of the gramicidin channel by divalent cations.J. Membrane Biol. 35:351–375
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