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Two possible conducting states of the influenza A virus M2 ion channel
Author(s) -
Zhong Qingfeng,
Newns Dennis M.,
Pattnaik Pratap,
Lear James D.,
Klein Michael L.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01522-2
Subject(s) - protonation , octane , chemistry , ion channel , conductance , helix (gastropod) , crystallography , stereochemistry , peptide , molecular dynamics , ion , computational chemistry , biochemistry , physics , organic chemistry , biology , ecology , receptor , snail , condensed matter physics
Molecular dynamics simulations have been performed on protonated four‐helix bundles based on the 25‐residue Duff–Ashley transmembrane sequence of the M2 channel of the influenza A virus. Well‐equilibrated tetrameric channels, with one, two and four of the H37 residues protonated, were investigated. The protonated peptide bundles were immersed in the octane portion of a phase‐separated water/octane system, which provided a membrane‐mimetic environment. The simulations suggest that there could be two conducting states of the M2 channel corresponding to tetramers containing one or two protonated histidines. The more open structure of the doubly protonated state suggests it would have the higher conductance.