Article
Molecular basis for nonadditive mutational effects in Escherichia coli dihydrofolate reductase.
Biochemistry - 5 Dec 1995
Wagner C R, Huang Z, Singleton S F, Benkovic S J
Abstract excerpt
Recently, two sets of single, double, and quadruple residue changes within the hydrophobic substrate binding pocket of Escherichia coli dihydrofolate reductase (5,6,7,8-tetrahydrofolate+ oxidoreductase, EC 1.5.1.3) were shown to exhibit nonadditive mutational effects [Huang, Z., Wagner, C. R., &...
Topics
- Base Sequence
- Binding Sites
- Catalysis
- Escherichia coli
- Kinetics
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Oligodeoxyribonucleotides
- Protein Conformation
- Tetrahydrofolate Dehydrogenase
- Thermodynamics