Folding mechanism of the α-subunit of tryptophan synthase, an α/β barrel protein: Global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels

Biochemistry

Volumn 38, Issue 3, 1999, Pages 1018-1029

  Bilsel, Osman ^a   Zitzewitz, Jill A ^a   Bowers, Katherine E ^a   Matthews, C Robert ^a  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

TRYPTOPHAN SYNTHASE; UREA;

ALPHA CHAIN; ARTICLE; CIRCULAR DICHROISM; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING;

CIRCULAR DICHROISM; DOSE-RESPONSE RELATIONSHIP, DRUG; ESCHERICHIA COLI; KINETICS; MODELS, CHEMICAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS; TRYPTOPHAN SYNTHASE; UREA;

ESCHERICHIA COLI;

EID: 0033579862     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi982365q     Document Type: Article

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