Detecting the inter-peptide arrangement and maturation process of transthyretin (105-115) amyloid fibril using a FRET pair with short Förster distance

Biochemical and Biophysical Research Communications

Volumn 362, Issue 3, 2007, Pages 689-694

  Deng, Wei ^a   Cao, Aoneng ^a   Lai, Luhua ^a  

^a PEKING UNIVERSITY   (China)

Author keywords

Amyloid fibril formation; Amyloid fibril structure; Electron microscope; FRET; Parallel sheet; Transthyretin (105 115)

Indexed keywords

AMYLOID; PREALBUMIN; TRANSTHYRETIN[105-115]; TRYPTOPHAN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; ELECTRON MICROSCOPY; FLUORESCENCE RESONANCE ENERGY TRANSFER; MOLECULAR PROBE; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN SYNTHESIS;

AMYLOID; AMYLOIDOSIS; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMANS; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MICROSCOPY, ELECTRON, TRANSMISSION; PEPTIDES; PREALBUMIN; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SPECTROPHOTOMETRY;

EID: 34548400699     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.08.059     Document Type: Article

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