Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain

Protein Science

Volumn 10, Issue 12, 2001, Pages 2541-2547

  Chiti, Fabrizio ^a   Bucciantini, Monica ^a   Capanni, Cristina ^a   Taddei, Niccoló ^a   Dobson, Christopher M ^b   Stefani, Massimo ^a  

^a UNIVERSITY OF FLORENCE   (Italy)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Aggregation; Amyloid fibrils; HypF N terminal domain; Protofilaments; Trifluoroethanol

Indexed keywords

AMYLOID; TRIFLUOROETHANOL;

ACIDITY; AMINO TERMINAL SEQUENCE; ARTICLE; CONCENTRATION RESPONSE; ELECTRON MICROSCOPY; FIBER; HYDROPHOBICITY; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN INTERACTION;

AMYLOID; AMYLOID BETA-PROTEIN; BACTERIAL PROTEINS; CIRCULAR DICHROISM; CLONING, MOLECULAR; COLORING AGENTS; CONGO RED; ESCHERICHIA COLI; FLUORESCENT DYES; HEAT; HYDROGEN-ION CONCENTRATION; MICROSCOPY, ELECTRON; PROTEIN STRUCTURE, TERTIARY; THIAZOLES; TIME FACTORS; TRIFLUOROETHANOL; UREA;

EID: 0035187228     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.ps.10201     Document Type: Article

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