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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Cleveland, M. V. Slatin, S. Levinthal, C. Finkelstein, A. |
| Abstract | The effects on planar lipid bilayer membranes of carboxyl-terminal fragments derived from the bacteriocin colicin E1 by either proteolysis or CNBr cleavage are indistinguishable from those of the voltage-dependent parent colicin molecule. An upper limit to the length of the COOH-terminal peptide required for channel formation is 152 amino acid residues from the COOH-terminal end, as indicated by the CNBr fragment. In addition, use of carboxypeptidase shows that the COOH-terminal end of the molecule remains on the side of the membrane to which it was added. COOH-terminal peptides of colicin E1 spontaneously associate with oil or hexane droplets in an aqueous system and remain at the interface between the two phases to a significantly greater degree than other colicin E1 fragments or cytochrome c. These results, together with the amino acid sequence, suggest a model wherein the colicin E1 channel is formed first by spontaneous attachment to a membrane of an alpha-helical hairpin centered at a 35-residue hydrophobic region near the COOH-terminal end. Application of a potential of the correct polarity then facilitates a major conformational change in the protein, allowing insertion of the remainder of the COOH-terminal end to form the open channel. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 12 |
| Volume Number | 80 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1983-07-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Colicins Ion Channels Metabolism Lipid Bilayers Isolation & Purification Cyanogen Bromide Endopeptidases Membrane Potentials Models, Biological Peptide Fragments Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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