DHPC Strongly Affects the Structure and Oligomerization Propensity of Alzheimer's Aβ(1-40) Peptide

Journal of Molecular Biology

Volumn 403, Issue 4, 2010, Pages 643-659

  Dahse, Kirsten ^a   Garvey, Megan ^b   Kovermann, Michael ^c   Vogel, Alexander ^c   Balbach, Jochen ^c   Fändrich, Marcus ^b,c   Fahr, Alfred ^a  

^a FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

^b MAX PLANCK RESEARCH UNIT FOR ENZYMOLOGY OF PROTEIN FOLDING   (Germany)

^c MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

Author keywords

Amyloid; Lipid; Oligomer; Prion; Protein misfolding

Indexed keywords

1,2 DIHEXANOYLGLYCERO 3 PHOSPHOCHOLINE; AMYLOID BETA PROTEIN[1-40]; GLYCEROL DERIVATIVE; PHOSPHORYLCHOLINE; UNCLASSIFIED DRUG; 1,2-DIHEXADECYL-SN-GLYCERO-3-PHOSPHOCHOLINE; AMYLOID BETA PROTEIN; ETHER PHOSPHOLIPID; MICELLE; PEPTIDE FRAGMENT;

ALZHEIMER DISEASE; ARTICLE; BETA SHEET; FIBROGENESIS; MICELLE; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN INTERACTION; PROTEIN LIPID INTERACTION; PROTEIN STRUCTURE; AMINO ACID SEQUENCE; BIOPHYSICS; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HUMAN; IN VITRO STUDY; INFRARED SPECTROSCOPY; KINETICS; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; SOLUBILITY; SURFACE TENSION; TRANSMISSION ELECTRON MICROSCOPY; ULTRASTRUCTURE;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMYLOID BETA-PEPTIDES; BIOPHYSICAL PHENOMENA; HUMANS; IN VITRO TECHNIQUES; KINETICS; MICELLES; MICROSCOPY, ELECTRON, TRANSMISSION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PHOSPHOLIPID ETHERS; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; SOLUBILITY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; SURFACE TENSION;

EID: 77957901872     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.09.021     Document Type: Article

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