The conserved phenylalanine in the K+ channel voltage-sensor domain creates a barrier with unidirectional effects

Biophysical Journal

Volumn 104, Issue 1, 2013, Pages 75-84

  Schwaiger, Christine S ^a   Liin, Sara I ^b   Elinder, Fredrik ^b   Lindahl, Erik ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

^b LINKÖPING UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; PHENYLALANINE; SHAKER POTASSIUM CHANNEL;

ANIMAL; ARTICLE; CHANNEL GATING; CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; KINETICS; METABOLISM; MUTATION; NUCLEOTIDE SEQUENCE; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; STRUCTURE ACTIVITY RELATION; XENOPUS;

ANIMALS; CONSERVED SEQUENCE; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; ION CHANNEL GATING; KINETICS; MODELS, MOLECULAR; MUTANT PROTEINS; MUTATION; PHENYLALANINE; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SHAKER SUPERFAMILY OF POTASSIUM CHANNELS; STRUCTURE-ACTIVITY RELATIONSHIP; XENOPUS;

EID: 84872151920     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.11.3827     Document Type: Article

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