Beta-strand interfaces of non-dimeric protein oligomers are characterized by scattered charged residue patterns

PLoS ONE

Volumn 7, Issue 4, 2012, Pages

  Feverati, Giovanni ^a   Achoch, Mounia ^a,b   Zrimi, Jihad ^a,b   Vuillon, Laurent ^a   Lesieur, Claire ^a,c  

^a UNIVERSITÉ DE SAVOIE   (France)

^b FACULTÉ DES SCIENCES ET TECHNIQUES GUÉLIZ   (Morocco)

^c UNIV GRENOBLE ALPES   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; ARGININE; CHOLERA TOXIN B SUBUNIT; GLUTAMIC ACID; HISTIDINE; NON DIMERIC PROTEIN OLIGOMER; OLIGOMER; UNCLASSIFIED DRUG; AMINO ACID; PEPTIDE FRAGMENT; PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; GEOMETRY; HYDROPHOBICITY; MOLECULAR INTERACTION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN ANALYSIS; PROTEIN SECONDARY STRUCTURE; STOICHIOMETRY; CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER PROGRAM; HUMAN; HYDROGEN BOND; METABOLISM; PROTEIN FOLDING; PROTEIN MULTIMERIZATION;

AMINO ACIDS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HUMANS; HYDROGEN BONDING; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MODELS, MOLECULAR; PEPTIDE FRAGMENTS; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PROTEINS; SOFTWARE;

EID: 84859509789     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0032558     Document Type: Article

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