Article
Changes in crystallographic structure and thermostability of a Cu,Zn superoxide dismutase mutant resulting from the removal of a buried cysteine.
The Journal of biological chemistry - 25 Aug 1990
McRee D E, Redford S M, Getzoff E D, Lepock J R, Hallewell R A, Tainer J A
Abstract excerpt
In principle, protein thermostability depends on efficient interior packing of apolar residues and on avoidance of irreversible denaturation in the unfolded state. To study these effects, the single free cysteine in the highly stable enzyme bovine Cu,Zn superoxide dismutase was mutated to alanine...
Topics
- Alanine
- Amino Acid Sequence
- Animals
- Calorimetry, Differential Scanning
- Cattle
- Crystallization
- Cysteine
- Enzyme Stability
- Hot Temperature
- Kinetics
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Superoxide Dismutase
- X-Ray Diffraction