Changing Val-76 towards Kir channels drastically influences the folding and gating properties of the bacterial potassium channel KcsA

Biophysical Chemistry

Volumn 144, Issue 3, 2009, Pages 95-100

  Raja, Mobeen ^a   Vales, Elisabeth ^a  

^a JOHANNES KEPLER UNIVERSITY LINZ   (Austria)

Author keywords

Mutation; Planar lipid bilayer; Potassium channels; Protein folding; Selectivity filter; Tetrameric stability; Tryptophan fluorescence

Indexed keywords

ACRYLAMIDE; INWARDLY RECTIFYING POTASSIUM CHANNEL; ISOLEUCINE; POTASSIUM CHANNEL; POTASSIUM CHANNEL KCSA; TRYPTOPHAN; UNCLASSIFIED DRUG; VALINE;

ARTICLE; CHANNEL GATING; CONTROLLED STUDY; HYDROPHILICITY; LIPID BILAYER; NONHUMAN; POTASSIUM CONDUCTANCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN MODIFICATION;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; ESCHERICHIA COLI; HYDROPHOBICITY; KINETICS; LIPID BILAYERS; MEMBRANE POTENTIALS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; POTASSIUM CHANNELS; POTASSIUM CHANNELS, INWARDLY RECTIFYING; PROBABILITY; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; SEQUENCE HOMOLOGY, AMINO ACID; TRYPTOPHAN;

BACTERIA (MICROORGANISMS);

EID: 69249203449     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2009.06.006     Document Type: Article

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