Article
Construction and characterization of a single polypeptide chain containing two enzymatically active dihydrofolate reductase domains.
Protein engineering - 1 Dec 1992
Iwakura M, Matthews C R
Abstract excerpt
A single polypeptide chain containing two dihydrofolate reductase (DHFR) sequences from Escherichia coli was constructed to determine if a repeat sequence fusion protein could be expressed in an active form. The possibility that intersequence interactions could play a significant role for this enzyme is suggested by the results of Hall and Frieden (1989, Proc. Natl Acad. Sci. USA, 86, 3060-3064) who observed a...
Topics
- Amino Acid Sequence
- Base Sequence
- Enzyme Stability
- Escherichia coli
- Genetic Engineering
- Molecular Sequence Data
- Molecular Weight
- Mutation
- Protein Conformation
- Protein Folding
- Recombinant Fusion Proteins
