Helical secondary structure of the external S3-S4 linker of pacemaker (HCN) channels revealed by site-dependent perturbations of activation phenotype

Journal of Biological Chemistry

Volumn 278, Issue 25, 2003, Pages 22290-22297

  Lesso, Heinte ^b   Li, Ronald A ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

ALGORITHMS; CHEMICAL ACTIVATION; CONFORMATIONS; PERTURBATION TECHNIQUES; REACTION KINETICS;

HELICAL STRUCTURES;

BIOCHEMISTRY;

AMINO ACID; GLUTAMIC ACID; GLYCINE; HCN S3 S4 LINKER PROTEIN; HYPERPOLARIZATION ACTIVATED CYCLIC NUCLEOTIDE MODULATED PROTEIN; METHIONINE; UNCLASSIFIED DRUG;

ALGORITHM; ARTICLE; CHANNEL GATING; DEPOLARIZATION; KINETICS; MEMBRANE CHANNEL; MEMBRANE CURRENT; MODEL; MUTATION; PACEMAKER CHANNEL; PHENOTYPE; PREDICTION; PRIORITY JOURNAL; PROTEIN ACTIVATION PHENOTYPE; PROTEIN CONFORMATION; PROTEIN FAMILY; PROTEIN SECONDARY STRUCTURE; STRUCTURE ACTIVITY RELATION; SURFACE CHARGE;

ALGORITHMS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; CLONING, MOLECULAR; ION CHANNELS; MEMBRANE POTENTIALS; MICE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NERVE TISSUE PROTEINS; PATCH-CLAMP TECHNIQUES; POLYMERASE CHAIN REACTION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SEQUENCE DELETION;

EID: 0038492590     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M302466200     Document Type: Article

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