Article
A thermostable mutation located at the hydrophobic core of alpha 1-antitrypsin suppresses the folding defect of the Z-type variant.
The Journal of biological chemistry - 14 Apr 1995
Kim J, Lee K N, Yi G S, Yu M H
Abstract excerpt
A thermostable mutation, F51L, at the hydrophobic core of human alpha 1-antitrypsin (alpha 1AT) increased the conformational stability of the molecule by decreasing the unfolding rate significantly without altering the refolding rate. The mutation specifically influenced the transition between the native state and a compact intermediate, which retained approximately 70% of the far-UV CD signal, but which had most...
Topics
- Enzyme Stability
- Kinetics
- Mutation
- Protein Conformation
- Protein Folding
- Temperature
- Thermodynamics
- alpha 1-Antitrypsin