The C-terminal t peptide of acetylcholinesterase forms an αhelix that supports homomeric and heteromeric interactions

European Journal of Biochemistry

Volumn 271, Issue 1, 2004, Pages 33-47

  Bon, Suzanne ^a   Dufourcq, Jean ^b   Leroy, Jacqueline ^a   Cornut, Isabelle ^b   Massoulié, Jean ^a  

^a ECOLE NORMALE SUPÉRIEURE   (France)

^b CENTRE DE RECHERCHE PAUL PASCAL   (France)

Author keywords

Acetylcholinesterase; Amphiphilic alpha helix; Disulfide bonds; Proline rich domain

Indexed keywords

ACETYLCHOLINESTERASE; LIPID; PEPTIDE;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; DISULFIDE BOND; ENZYME STRUCTURE; HYDROPHOBICITY; MICELLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; SPECTROSCOPY;

ACETYLCHOLINESTERASE; AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES; ELECTROPHORUS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY;

HOMO; TORPEDO;

EID: 1642458122     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03892.x     Document Type: Article

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