Charge states rather than propensity for β-structure determine enhanced fibrillogenesis in wild-type Alzheimer's β-amyloid peptide compared to E22Q Dutch mutant

Protein Science

Volumn 11, Issue 7, 2002, Pages 1639-1647

  Massi, Francesca ^a   Klimov, D ^b   Thirumalai, D ^b   Straub, John E ^a  

^a USA   (United States)

^b University of Maryland   (United States)

Author keywords

A peptide; Aggregation; Amyloid; Amyloidosis; Conformational analysis; E22Q Dutch mutant peptide; Hydration; Molecular dynamics simulation

Indexed keywords

AMYLOID BETA PROTEIN; MUTANT PROTEIN; AMYLOID BETA PROTEIN (10 35); AMYLOID BETA-PROTEIN (10-35); PEPTIDE FRAGMENT;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AQUEOUS SOLUTION; ARTICLE; HYDRATION; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR DYNAMICS; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN STRUCTURE; AMINO ACID SUBSTITUTION; CHEMISTRY; COMPUTER SIMULATION; ELECTROPHYSIOLOGY; GENETICS; MUTATION; PHYSIOLOGY; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SUBSTITUTION; AMYLOID BETA-PROTEIN; COMPUTER SIMULATION; ELECTROPHYSIOLOGY; HYDROGEN BONDING; MUTATION; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 0036081257     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.3150102     Document Type: Article

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