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Bacterial α-hemolysin forms a pore in a lipid membrane with well-behaved single-channel conductance so that the transit of single molecules can be studied. Here we demonstrate that the structure of individual peptides can be analyzed. Peptides were synthesized containing repeats of the sequence (Gly−Pro−Pro), which exist as mixtures of single, double, or collagen-like triple helices. The structure of individual peptides could be identified as they traverse the pore based on signature transit times and blockage currents.
Sutherland et al. (Wed,) studied this question.
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