Double gaps along Shaker S4 demonstrate omega currents at three different closed states

Channels

Volumn 4, Issue 2, 2010, Pages 93-100

  Gamal El Din, Tamer M ^a   Heldstab, Hansjakob ^a   Lehmann, Claudia ^a   Greeff, Nikolaus G ^a  

^a UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

Channel conformation; Channel gating; Ion channel; Omega current; S4; Shaker potassium channel; Voltage sensor

Indexed keywords

AMINO ACID; ARGININE; SHAKER POTASSIUM CHANNEL; ALANINE; POTASSIUM; PROTEIN SUBUNIT; SERINE;

ALPHA HELIX; ARTICLE; CHANNEL GATING; ELECTRIC POTENTIAL; MUTATION; SENSOR; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; KINETICS; MEMBRANE POTENTIAL; METABOLISM; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; PROTEIN SUBUNIT; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; XENOPUS;

ALANINE; AMINO ACIDS; ANIMALS; ARGININE; ION CHANNEL GATING; KINETICS; MEMBRANE POTENTIALS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; POTASSIUM; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS; SERINE; SHAKER SUPERFAMILY OF POTASSIUM CHANNELS; STRUCTURE-ACTIVITY RELATIONSHIP; XENOPUS;

EID: 77953560367     PISSN: 19336950     EISSN: 19336969     Source Type: Journal    
DOI: 10.4161/chan.4.2.10672     Document Type: Article

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