Structural and functional changes in a synthetic S5 segment of KvLQT1 channel as a result of a conserved amino acid substitution that occurs in LQT1 syndrome of human

Biochimica et Biophysica Acta - Biomembranes

Volumn 1798, Issue 3, 2010, Pages 461-470

  Verma, Richa ^a   Ghosh, Jimut Kanti ^a  

^a CENTRAL DRUG RESEARCH INSTITUTE   (India)

Author keywords

Assembly of synthetic S5; Cardiac voltage gated potassium channel KvLQT1; Long QT syndrome; LQTS1 associated mutation; Peptide membrane interaction; Pore forming activity of S5 peptide in phospholipid vesicle; Voltage gated potassium channel

Indexed keywords

GLYCINE; POTASSIUM CHANNEL KV1.1; SERINE;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ENERGY TRANSFER; FLUORESCENCE ANALYSIS; GENE FUNCTION; GENE LOCATION; GENE STRUCTURE; GENETIC CONSERVATION; HUMAN; LIPID MEMBRANE; LONG QT SYNDROME; MEMBRANE BINDING; MOLECULAR PROBE; NONHUMAN; PEPTIDE ANALYSIS; PHOSPHOLIPID VESICLE; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN SECONDARY STRUCTURE; WILD TYPE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CONSERVED SEQUENCE; ENDOPEPTIDASE K; FLUORESCENCE; HUMANS; KCNQ1 POTASSIUM CHANNEL; LIPOSOMES; LONG QT SYNDROME; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; MUTATION; OXADIAZOLES; PEPTIDES; PERMEABILITY; PHOSPHATIDYLCHOLINES; PHOSPHATIDYLGLYCEROLS; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 76749171131     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2009.12.014     Document Type: Article

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