Folding, stability, and physical properties of the α subunit of bacterial luciferase

Biochemistry

Volumn 38, Issue 49, 1999, Pages 16136-16145

  Noland, Brian W ^a   Dangott, Lawrence J ^a   Baldwin, Thomas O ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; LUCIFERASE; PHOSPHATE; SODIUM CHLORIDE; UREA;

AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; DISSOCIATION CONSTANT; ENZYME ANALYSIS; ENZYME DENATURATION; ENZYME STABILITY; ENZYME SUBUNIT; ESCHERICHIA COLI; FLUORESCENCE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; ULTRACENTRIFUGATION; VIBRIO HARVEYI;

CHEMISTRY, PHYSICAL; CIRCULAR DICHROISM; DIMERIZATION; ENDOPEPTIDASES; HYDROLYSIS; LUCIFERASES; MODELS, MOLECULAR; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, FLUORESCENCE; ULTRACENTRIFUGATION; UREA;

EID: 0033534148     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi991449b     Document Type: Article

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