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Collective behavior of S6 peptide channels derived from KvAP (a bacterial potassium channel) incorporated in lipid bilayer membrane, has been investigated at various applied potentials through multi-channel electrophysiological experiments. The current versus time traces at any particular membrane potential show clear steps for sequential opening of the multi-channels. The minimum current (representing one-channel current) was found out from the amplitude histograms. Accordingly, the number of open channels corresponding to a particular open state was calculated. It was observed that the above-mentioned one channel current is higher than the corresponding single-channel current at most of the applied membrane potentials. Moreover, the difference between the single and one channel conductances is a nonlinear function of the membrane potential. We conclude that the S6 multi-channels show co-operative gating. Voltage relaxation studies support the above-mentioned conclusion.

S6 Peptide Derived from KvAP Channel Shows Cooperativity in Gating on Bilayer Lipid Membrane