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©2014 Author(s). Published by the American Society for Microbiology. This is an Open Access article distributed under the terms of the a Creative Commons Attribution – Noncommercial – Share Alike 3.0 Unported License (http://creativecommons.org/licenses/by-nc-sa/3.0/), which permits unrestricted non-commercial use and distribution, provided the original(More)
Channel-forming colicins exist in at least two different membrane-associated conformations: a voltage-independent closed-channel state and a voltage-dependent open-channel state. In a voltage-independent membrane-associated conformation, we find that two major regions of colicin Ia are protected from pepsin proteolysis after association with negatively(More)
Filipin, a polyene antibiotic, interacts with beta-hydroxy sterols such as cholesterol in most cell membranes, forming bumps and pits that are visible by electron microscopy of freeze-fracture replicas. The markedly reduced perturbability of the red blood cell (RBC) membrane, compared to other cells, has been attributed to the constraining influence of the(More)
Colicin Ia, a member of the channel-forming family of colicins, inserts into model membranes in a pH- and lipid-dependent fashion. This insertion occurs with single-hit kinetics, requires negatively charged lipids in the target membrane, and increases in rate as the pH is reduced below 5.2. The low-pH requirement does not act by inducing a secondary(More)
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