The aggregation kinetics of Alzheimer's β-amyloid peptide is controlled by stochastic nucleation

Protein Science

Volumn 14, Issue 7, 2005, Pages 1753-1759

  Hortschansky, Peter ^b   Schroeckh, Volker ^b   Christopeit, Tony ^a   Zandomeneghi, Giorgia ^a   Fändrich, Marcus ^a  

^a FRITZ LIPMANN INSTITUTE   (Germany)

^b HANS KNÖLL INSTITUTE   (Germany)

Author keywords

Amyloid; Conformational disease; Kinetics; Prion; Protein folding

Indexed keywords

AMYLOID BETA PROTEIN; BUFFER; SODIUM DIHYDROGEN PHOSPHATE; WATER;

ALZHEIMER DISEASE; ARTICLE; CHEMICAL REACTION KINETICS; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; NONHUMAN; OLIGOMERIZATION; PHYSICAL CHEMISTRY; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN SECRETION; TIME;

AMYLOID BETA-PROTEIN; CIRCULAR DICHROISM; COMPUTER SIMULATION; ENDOPEPTIDASES; HISTIDINE; HUMANS; KINETICS; MUTATION; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN FOLDING; SOLUBILITY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; THIAZOLES;

EID: 22244439242     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.041266605     Document Type: Article

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