The role of protein stability, solubility, and net charge in amyloid fibril formation

Protein Science

Volumn 12, Issue 10, 2003, Pages 2374-2378

  Schmittschmitt, Jason P ^a   Scholtz, J Martin ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

Author keywords

Amyloid; Amyloid fibrils; pI; Protein solubility; Protein stability

Indexed keywords

AMYLOID; PROTEIN; TRIFLUOROETHANOL;

AMINO ACID SEQUENCE; ARTICLE; CORRELATION ANALYSIS; PH; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STABILITY; SOLUBILITY; SYNTHESIS;

AMYLOID; CIRCULAR DICHROISM; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; ISOENZYMES; POINT MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; RIBONUCLEASES; SOLUBILITY; SPECTROMETRY, FLUORESCENCE; STREPTOMYCES AUREOFACIENS; THERMODYNAMICS; THIAZOLES; TRIFLUOROETHANOL;

EID: 0141746349     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03152903     Document Type: Article

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