Article
The hydrophobic core of Escherichia coli thioredoxin shows a high tolerance to nonconservative single amino acid substitutions.
Biochemistry - 17 Nov 1992
Hellinga H W, Wynn R, Richards F M
Abstract excerpt
A set of single amino acid substitutions has been constructed at positions Leu42 and Leu78 in the hydrophobic core of Escherichia coli thioredoxin. This protein is required for the in vivo assembly of filamentous bacteriophages such as M13. Almost all the mutants retain this activity regardless of the change in size, hydrophobic nature, or charge of the substitution. Determination of the free energies of...
Topics
- Amino Acids
- Circular Dichroism
- Escherichia coli
- Mutation
- Protein Folding
- Thermodynamics
- Thioredoxins