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Volumn 511, Issue 1-3, 2002, Pages 159-164
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Charge conversion enables quantification of the proximity between a normally-neutral μ-conotoxin (GIIIA) site and the Na+ channel pore
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Author keywords
Conotoxin; Mutagenesis; Mutant cycle analysis; Protein engineering; Sodium channel
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Indexed keywords
ALANINE;
CONOTOXIN;
GLUTAMIC ACID;
ION CHANNEL;
RECEPTOR PROTEIN;
RECEPTOR SUBUNIT;
SODIUM CHANNEL;
SODIUM ION;
ANIMAL TISSUE;
ARTICLE;
CARBOXY TERMINAL SEQUENCE;
CONTROLLED STUDY;
NONHUMAN;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN INTERACTION;
PROTEIN STRUCTURE;
PROTEIN SYNTHESIS;
RAT;
SODIUM TRANSPORT;
STRAIN DIFFERENCE;
ALANINE;
AMINO ACID SUBSTITUTION;
ANIMALS;
BINDING SITES;
CONOTOXINS;
ELECTROPHYSIOLOGY;
ELECTROSTATICS;
GLUTAMIC ACID;
KINETICS;
MODELS, MOLECULAR;
MUSCLE, SKELETAL;
MUTAGENESIS, SITE-DIRECTED;
NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR;
PATCH-CLAMP TECHNIQUES;
PROTEIN BINDING;
PROTEIN CONFORMATION;
RATS;
SODIUM CHANNEL BLOCKERS;
SODIUM CHANNELS;
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EID: 0037196391
PISSN: 00145793
EISSN: None
Source Type: Journal
DOI: 10.1016/S0014-5793(01)03316-6 Document Type: Article |
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Times cited : (17)
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References (23)
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