Mutations alter the geometry and mechanical properties of Alzheimer's Aβ(1-40) amyloid fibrils

Biochemistry

Volumn 49, Issue 41, 2010, Pages 8967-8977

  Paparcone, Raffaella ^a   Pires, Matthew A ^a   Buehler, Markus J ^a,b  

^a USA   (United States)

^b MIT Energy Initiative   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; CHEMICAL STABILITY; DISEASE CONTROL; DISEASES; DRUG INTERACTIONS; DRUG THERAPY; FUNCTIONAL GROUPS; HYDROGEN BONDS; MECHANICAL PROPERTIES; MECHANICAL STABILITY; MECHANISMS; MOLECULAR DYNAMICS; REACTION KINETICS;

ALZHEIMER'S; ALZHEIMER'S DISEASE; AMYLOID FIBRIL; AMYLOID PLAQUES; AMYLOID STRUCTURES; BRAIN TISSUE; CHEMICAL DEACTIVATION; DEGENERATIVE DISEASE; DENSE NETWORK; DRUG DESIGN; DRUG DISCOVERY RESEARCHES; INNER CORE; MECHANICAL STIFFNESS; MOLECULAR DYNAMICS SIMULATIONS; MOLECULAR INSIGHTS; MOLECULAR THERAPY; PERIOD LENGTH; SALT BRIDGES; SCALE PROPERTIES; SIDE CHAINS; YOUNG'S MODULUS;

GLYCOPROTEINS;

AMYLOID BETA PROTEIN[1-40]; AMYLOID; AMYLOID BETA PROTEIN; PEPTIDE FRAGMENT;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; ARTICLE; GENE MUTATION; GEOMETRY; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN INTERACTION; PROTEIN STRUCTURE; YOUNG MODULUS; CHEMISTRY; GENETICS; METABOLISM; PROTEIN SECONDARY STRUCTURE;

ALZHEIMER DISEASE; AMYLOID; AMYLOID BETA-PEPTIDES; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY;

EID: 77957909677     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100953t     Document Type: Article

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