Aβ peptide fibrillar architectures controlled by conformational constraints of the monomer

PLoS ONE

Volumn 6, Issue 9, 2011, Pages

  Brännström, Kristoffer ^a   Öhman, Anders ^a   Olofsson, Anders ^a  

^a UMEÅ UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; MONOMER; SOLVENT;

ARTICLE; ATOMIC FORCE MICROSCOPY; BINDING AFFINITY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DEUTERIUM HYDROGEN EXCHANGE NUCLEAR MAGNETIC RESONANCE; ISOMERIZATION; MOLECULAR DOCKING; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; POLYMERIZATION; PROTEIN AGGREGATION; PROTEIN STRUCTURE; SURFACE PLASMON RESONANCE; THERMODYNAMICS; WILD TYPE;

AMYLOID BETA-PEPTIDES; MAGNETIC RESONANCE SPECTROSCOPY; MICROSCOPY, ATOMIC FORCE; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; SURFACE PLASMON RESONANCE;

RUMEX;

EID: 80053294730     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0025157     Document Type: Article

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