Dynamic properties of pH-dependent structural organization of the amyloidogenic β-protein (1-40)

Prion

Volumn 3, Issue 1, 2009, Pages 31-43

  Rubinstein, Alexander ^a,b   Lyubchenko, Yuri L ^a   Sherman, Simon ^a,c  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

^b UNIVERSITY OF NEBRASKA AT OMAHA   (United States)

^c NEBRASKA MEDICAL CENTER   (United States)

Author keywords

Alzheimer disease; Amyloid protein; Electrostatic interactions; Fibril; Molecular dynamics simulations; Oligomerization

Indexed keywords

ALANINE; AMYLOID BETA PROTEIN[1-40]; GLUTAMIC ACID; GLYCINE; PHENYLALANINE;

ACIDITY; ALPHA HELIX; ARTICLE; CONTROLLED STUDY; ELECTRICITY; HIGH TEMPERATURE; HYDROGEN BOND; MOLECULAR DYNAMICS; OLIGOMERIZATION; PH; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN DETERMINATION; PROTEIN FOLDING; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; SIMULATION; STRUCTURE ANALYSIS;

AMINO ACIDS; AMYLOID BETA-PROTEIN; CLUSTER ANALYSIS; COMPUTER SIMULATION; HOT TEMPERATURE; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; PEPTIDE FRAGMENTS; PHYSICOCHEMICAL PHENOMENA; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; STATIC ELECTRICITY;

EID: 66749136907     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.3.1.8388     Document Type: Article

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