Polymorphic triple β-sheet structures contribute to amide hydrogen/deuterium (H/D) exchange protection in the Alzheimer amyloid β42 peptide

Journal of Biological Chemistry

Volumn 286, Issue 39, 2011, Pages 34244-34253

  Ma, Buyong ^a   Nussinov, Ruth ^a,b  

^a NATIONAL CANCER INSTITUTE   (United States)

^b TEL AVIV UNIVERSITY   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER AMYLOID; ALZHEIMER DISEASE; AMIDE HYDROGENS; COMPUTATIONAL MODELING; CONFORMATIONAL ENSEMBLE; H/D EXCHANGE; HYDROPHOBIC RESIDUES; N-TERMINALS; NMR SOLVENTS; PENTAMERS; PROTECTION RATIOS; SHEET FIBRILS; SHEET STRUCTURE; STRUCTURAL ELUCIDATION; STRUCTURAL MOTIFS; STRUCTURAL SIMILARITY;

AMIDES; OLIGOMERS;

GLYCOPROTEINS;

AMYLOID BETA PROTEIN[1-42];

ALZHEIMER DISEASE; AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; CONFORMATION; CONTROLLED STUDY; DEUTERIUM HYDROGEN EXCHANGE; HYDROPHOBICITY; MOLECULAR DYNAMICS; MUTANT; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN STRUCTURE; SIMULATION;

ALZHEIMER DISEASE; AMYLOID; AMYLOID BETA-PEPTIDES; DEUTERIUM EXCHANGE MEASUREMENT; HUMANS; MODELS, CHEMICAL; MUTATION; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY;

EID: 80053203496     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.241141     Document Type: Article

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