Effects of the difference in the unfolded-state ensemble on the folding of Escherichia coli dihydrofolate reductase

Journal of Molecular Biology

Volumn 329, Issue 4, 2003, Pages 779-791

  Arai, Munehito ^a,b   Kataoka, Mikio ^c   Kuwajima, Kunihiro ^b   Matthews, C Robert ^d   Iwakura, Masahiro ^a  

^a NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

^d UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

Circular protein; Dihydrofolate reductase; Folding intermediate; Protein folding; Unfolded state

Indexed keywords

DIHYDROFOLATE REDUCTASE; PROTEIN;

ABSORPTION SPECTROPHOTOMETRY; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHEMICAL REACTION KINETICS; CIRCULAR DICHROISM; COMPARATIVE STUDY; CROSS LINKING; DISULFIDE BOND; ENTROPY; ESCHERICHIA COLI; FLUORESCENCE; GEL PERMEATION CHROMATOGRAPHY; MEASUREMENT; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; RADIATION SCATTERING;

ESCHERICHIA COLI;

EID: 0038730768     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00511-4     Document Type: Article

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