Unusual property of prion protein unfolding in neutral salt solution

Biochemistry

Volumn 41, Issue 36, 2002, Pages 11017-11024

  Nandi, P K ^a   Leclerc, E ^b   Marc, D ^a  

^a CEMAGREF   (France)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PRION DISEASES;

AMINO ACIDS; NEGATIVE IONS; NUCLEIC ACIDS; SALTS;

PROTEINS;

ANION; CELL PROTEIN; FLUORIDE; GLYCINE; GLYCOSAMINOGLYCAN; NUCLEIC ACID; PRION PROTEIN; SODIUM CHLORIDE; SULFATE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DENATURATION; NONHUMAN; PRION DISEASE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; SOLUBILITY;

AMINO ACID SEQUENCE; ANIMALS; BUFFERS; CIRCULAR DICHROISM; HEAT; HYDROGEN-ION CONCENTRATION; MICE; MOLECULAR SEQUENCE DATA; MURAMIDASE; PEPTIDE FRAGMENTS; PRIONS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SALTS; SHEEP; SOLUTIONS; SPECTROMETRY, FLUORESCENCE; SULFATES; TRYPTOPHAN;

OVIS ARIES;

EID: 0036713563     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi025886t     Document Type: Article

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