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Science 12 February 1993:
Vol. 259. no. 5097, pp. 960 - 963
DOI: 10.1126/science.8382373
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Articles
Science, Vol 259, Issue 5097, 960-963
Copyright © 1993 by American Association for the Advancement of Science
Colicin E1 binding to membranes: time-resolved studies of spin-labeled mutants
YK Shin,
C Levinthal,
F Levinthal,
and
WL Hubbell
Jules Stein Eye Institute, University of California, Los Angeles 90024.
To investigate the mechanism of interaction of the toxin colicin E1 with membranes, three cysteine substitution mutants and the wild type of the channel-forming fragment were spin labeled at the unique thiol. Time-resolved interaction of these labeled proteins with phospholipid vesicles was investigated with stopped-flow electron paramagnetic resonance spectroscopy. The fragment interacts with neutral bilayers at low pH, indicating that the interaction is hydrophobic rather than electrostatic. The interaction occurs in at least two distinct steps: (i) rapid adsorption to the surface; and (ii) slow, rate-limiting insertion of the hydrophobic central helices into the membrane interior.
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