Salt anions promote the conversion of HypF-N into amyloid-like oligomers and modulate the structure of the oligomers and the monomeric precursor state

Journal of Molecular Biology

Volumn 424, Issue 3-4, 2012, Pages 132-149

  Campioni, Silvia ^a   Mannini, Benedetta ^a   López Alonso, Jorge P ^b   Shalova, Irina N ^c   Penco, Amanda ^d   Mulvihill, Estefania ^a   Laurents, Douglas V ^b   Relini, Annalisa ^d   Chiti, Fabrizio ^a  

^a UNIVERSITY OF FLORENCE   (Italy)

^b INSTITUTO DE QUÍMICA FÍSICA ROCASOLANO   (Spain)

^c MOSCOW STATE UNIVERSITY   (Russian Federation)

^d UNIVERSITY OF GENOA   (Italy)

Author keywords

amyloid oligomers; conformational changes; oligomerization rate; polymorphism; salt ions

Indexed keywords

AMYLOID; ANION; BACTERIAL PROTEIN; CATION; HYPF N PROTEIN; LITHIUM CHLORIDE; MONOMER; OLIGOMER; POTASSIUM CHLORIDE; SODIUM CHLORIDE; SODIUM IODIDE; SODIUM SULFATE; UNCLASSIFIED DRUG;

ACIDITY; AMINO TERMINAL SEQUENCE; ARTICLE; ESCHERICHIA COLI; HYDROPHOBICITY; MACROMOLECULE; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN STRUCTURE;

ESCHERICHIA COLI;

EID: 84869083333     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.09.023     Document Type: Article

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