Dimer formation enhances structural differences between amyloid β-protein (1-40) and (1-42): An explicit-solvent molecular dynamics study

PLoS ONE

Volumn 7, Issue 4, 2012, Pages

  Barz, Bogdan ^a   Urbanc, Brigita ^a  

^a DREXEL UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; DIMER; MONOMER; OLIGOMER; SOLVENT; WATER; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN (1 42); AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT;

ALZHEIMER DISEASE; AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; DIMERIZATION; ENERGY; MOLECULAR DYNAMICS; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN STRUCTURE; SURFACE CHARGE; TOXICITY; AMINO ACID SEQUENCE; CHEMISTRY; COMPARATIVE STUDY; HYDROGEN BOND; MOLECULAR GENETICS; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; STATIC ELECTRICITY; THERMODYNAMICS;

AMINO ACID SEQUENCE; AMYLOID BETA-PEPTIDES; HYDROGEN BONDING; MOLECULAR DYNAMICS SIMULATION; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; STATIC ELECTRICITY; THERMODYNAMICS; WATER;

EID: 84859605341     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0034345     Document Type: Article

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