Morphology and secondary structure of stable β-oligomers formed by amyloid peptide PrP(106-126)

Biochemistry

Volumn 48, Issue 25, 2009, Pages 5779-5781

  Walsh, Patrick ^a,b   Yau, Jason ^b   Simonetti, Karen ^a   Sharpe, Simon ^a,b  

^a HOSPITAL FOR SICK CHILDREN   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PEPTIDES; CIRCULAR DICHROISM; HUMAN PRION PROTEIN; HYDRODYNAMIC RADIUS; HYDROPHOBIC CORE; SECONDARY STRUCTURES; SOLID STATE NMR; THIOFLAVIN;

AMINES; DICHROISM; DYES; FLUID DYNAMICS; GLYCOPROTEINS; MORPHOLOGY;

OLIGOMERS;

AMYLOID PROTEIN; PRION PROTEIN; PRION PROTEIN 106 126; THIOFLAVINE; UNCLASSIFIED DRUG;

ARTICLE; ATOMIC FORCE MICROSCOPY; CIRCULAR DICHROISM; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; TRANSMISSION ELECTRON MICROSCOPY;

AMYLOID; CIRCULAR DICHROISM; HUMANS; MICROSCOPY, ATOMIC FORCE; MICROSCOPY, ELECTRON, TRANSMISSION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PRIONS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY;

EID: 67649573991     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9007319     Document Type: Article

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