ArticleBiophysical journal1996
Membrane binding of the colicin E1 channel: activity requires an electrostatic interaction of intermediate magnitude.
Article in Biophysical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 39 citations in OpenAlex.
- Fluorescence spectroscopy in thermodynamic and kinetic analysis of pH-dependent membrane protein insertion.Methods in enzymology · 2009Article
- Chemical and photochemical modification of colicin E1 and gramicidin A in bilayer lipid membranes.The Journal of membrane biology · 2004Article
- Tuning the membrane surface potential for efficient toxin import.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Membrane-bound state of the colicin E1 channel domain as an extended two-dimensional helical array.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers.Protein science : a publication of the Protein Society · 1998Article
- Channel formation by antiapoptotic protein Bcl-2.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Transmembrane insertion of the colicin Ia hydrophobic hairpin.The Journal of membrane biology · 1997Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In vitro channel activity of the C-terminal colicin E1 channel polypeptide under conditions of variable electrostatic interaction with synthetic lipid membranes showed distinct maxima with respect to pH and membrane surface potential. The membrane binding energy was determined from fluorescence quenching of the intrinsic tryptophans of the channel polypeptide by liposomes containing N-trinitrophenyl-phosphatidylethanolamine. Maximum in vitro colicin channel activity correlated with an intermediate magnitude of the electrostatic interaction. For conditions associated with maximum activity (40% anionic lipid, I = 0.12 M, pH 4.0), the free energy of binding was delta G approximately -9 kcal/mol, with nonelectrostatic and electrostatic components, delta Gnel approximately -5 kcal/mol and delta Gel approximately -4 kcal/mol, and an effective binding charge of +7 at pH 4.0. Binding of the channel polypeptide to negative membranes at pH 8 is minimal, whereas initial binding at pH 4 followed by a shift to pH 8 causes only 3-10% reversal of binding, implying that it is kinetically trapped, probably by a hydrophobic interaction. It was inferred that membrane binding and insertion involves an initial electrostatic interaction responsible for concentration and binding to the membrane surface. This is followed by insertion into the bilayer driven by hydrophobic forces, which are countered in the case of excessive electrostatic binding.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.