Stability and reversibility of thermal denaturation are greatly improved by limiting terminal flexibility of escherichia coli dihydrofolate reductase

Journal of Biochemistry

Volumn 119, Issue 3, 1996, Pages 414-420

  Iwakura, Masahiro ^a,b   Honda, Shinya ^b  

^a NATL INST FOR ADV INTERDISC RES   (Japan)

^b NATL INST BIOSCI HUM TECHNOL   (Japan)

Author keywords

Circularized protein; Dihydrofolate reductase; Escherichia coli; Reversibility; Thermal stability

Indexed keywords

BACTERIAL ENZYME; DIHYDROFOLATE REDUCTASE; GUANIDINE; MUTANT PROTEIN; RECOMBINANT DNA;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONTROLLED STUDY; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME STABILITY; ENZYME STRUCTURE; ESCHERICHIA COLI; GEL FILTRATION CHROMATOGRAPHY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; NONHUMAN; REDUCTION; STRUCTURE ACTIVITY RELATION; THERMOSTABILITY;

EID: 0029876467     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021257     Document Type: Article

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