J. O. Bullock studied how Colicin E1 forms ion-conducting channels in lipid bilayers. A 1983 study compared the complete protein with a fragment from its C-terminus, measuring both individual-channel and aggregate electrical behaviour.[ref]
Comparison of the macroscopic and single channel conductance properties of colicin E1 and its COOH-terminal tryptic peptide by J. O. Bullock and others. Journal of Biological Chemistry258, pp.9908–9912; Abstract and byline
The fragment retained properties very similar to those of the complete Colicin E1. Both forms could bind a lipid bilayer before a suitable membrane potential permitted conduction. Fragmentation therefore helped locate a functional region, while electrical measurements distinguished attachment from pore opening. These are separate experimental questions even though both involve the same protein at the same membrane.[ref]
Comparison of the macroscopic and single channel conductance properties of colicin E1 and its COOH-terminal tryptic peptide by J. O. Bullock and others. Abstract; terminal fragment and potential-dependent channel formation
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