Refolding of the Escherichia coli expressed extracellular domain of α7 nicotinic acetylcholine receptor. Cys116 mutation diminishes aggregation and stabilizes the β structure

European Journal of Biochemistry

Volumn 269, Issue 11, 2002, Pages 2801-2809

  Tsetlin, Victor I ^a   Dergousova, Natalia I ^a   Azeeva, Ekaterina A ^a   Kryukova, Elena V ^a   Kudelina, Irina A ^a   Shibanova, Elena D ^a   Kasheverov, Igor E ^a   Methfessel, Christoph ^b  

^a SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

^b Central Research   (Germany)

Author keywords

7 nicotinic acetylcholine receptor; CD spectroscopy; Cys116 mutation; Expression in Escherichia coli; Extracellular domains

Indexed keywords

ALPHA BUNGAROTOXIN; DODECYL SULFATE SODIUM; MUTANT PROTEIN; NICOTINIC RECEPTOR; RECEPTOR SUBUNIT;

ARTICLE; CONTROLLED STUDY; ESCHERICHIA COLI; EXTRACELLULAR SPACE; GEL PERMEATION CHROMATOGRAPHY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MOLECULAR WEIGHT; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN ISOLATION; PROTEIN STABILITY; PROTEIN STRUCTURE;

AMINO ACID SUBSTITUTION; ANIMALS; COBRA NEUROTOXINS; MUTATION; PROTEIN FOLDING; PROTEIN RENATURATION; PROTEIN STRUCTURE, TERTIARY; RATS; RECEPTORS, NICOTINIC; RECOMBINANT FUSION PROTEINS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; HOMO; NEGIBACTERIA;

EID: 0036271421     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.02961.x     Document Type: Article

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