Effects of five-tryptophan mutations on structure, stability and function of Escherichia coli dihydrofolate reductase

Journal of Biochemistry

Volumn 130, Issue 3, 2001, Pages 439-447

  Ohmae, E ^a   Sasaki, Y ^a   Gekko, K ^a  

^a HIROSHIMA UNIVERSITY   (Japan)

Author keywords

Dihydrofolate reductase; Enzyme function; Point mutations; Structural stability; Tryptophan residues

Indexed keywords

BACTERIAL ENZYME; DIHYDROFOLATE REDUCTASE; LEUCINE; PEPTIDE; PHENYLALANINE; SOLVENT; TRYPTOPHAN; VALINE;

ARTICLE; CIRCULAR DICHROISM; ENERGY; ENZYME ACTIVITY; ENZYME STABILITY; ENZYME STRUCTURE; ESCHERICHIA COLI; FLUORESCENCE; NONHUMAN; POINT MUTATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0034848452     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a003004     Document Type: Article

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