The barriers in the bimolecular and unimolecular folding reactions of the dimeric core domain of Escherichia coli Trp repressor are dominated by enthalpic contributions

Biochemistry

Volumn 37, Issue 45, 1998, Pages 16000-16010

  Gloss, Lisa M ^a,b   Matthews, C Robert ^a  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

^b WASHINGTON STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

REPRESSOR PROTEIN;

ALPHA HELIX; ARTICLE; DIMERIZATION; ENTHALPY; ENTROPY; ESCHERICHIA COLI; FLUORESCENCE ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; REACTION ANALYSIS; REPRESSOR GENE; SURFACE PROPERTY; TEMPERATURE DEPENDENCE;

BACTERIAL PROTEINS; DIMERIZATION; ESCHERICHIA COLI; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; REPRESSOR PROTEINS; SOLVENTS; SPECTROMETRY, FLUORESCENCE; SURFACE PROPERTIES; TEMPERATURE; THERMODYNAMICS; TRYPTOPHAN;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0032506169     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi981694f     Document Type: Article

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