Article
A soluble immunoglobulin variable domain without a disulfide bridge: construction, accumulation in the cytoplasm of E. coli, purification and physicochemical characterization.
Biological chemistry Hoppe-Seyler - 1 May 1994
Frisch C, Kolmar H, Fritz H J
Abstract excerpt
Two amino acid exchanges (Y32H and C23V) were introduced sequentially into the immunoglobulin REIV, a human kappa variable domain. The first exchange stabilizes the folded state of the domain by 4.6 kJ/mol (1.1 kcal/mol), the second abolishes the central disulfide bridge and destabilizes the fold...
Topics
- Base Sequence
- Circular Dichroism
- Cloning, Molecular
- Disulfides
- Electrophoresis, Polyacrylamide Gel
- Escherichia coli
- Humans
- Immunoglobulin Variable Region
- Molecular Sequence Data
- Mutation
- Protein Conformation