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S6 peptide derived from KvAP channel shows cooperativity in gating on bilayer lipid membrane.

ABSTRACT: 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.

SUBMITTER: Malik C

PROVIDER: S-EPMC3827124 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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S6 peptide derived from KvAP channel shows cooperativity in gating on bilayer lipid membrane.

Malik Chetan C Ghosh Subhendu S

PloS one 20131112 11

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 o ...[more]

PMID: 24265723

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