Changes in crystallographic structure and thermostability of a Cu,Zn superoxide dismutase mutant resulting from the removal of a buried cysteine.

@article{McRee1990ChangesIC,
  title={Changes in crystallographic structure and thermostability of a Cu,Zn superoxide dismutase mutant resulting from the removal of a buried cysteine.},
  author={Duncan E. McRee and S M Redford and Elizabeth D. Getzoff and James R. Lepock and R. A. Hallewell and John A. Tainer},
  journal={The Journal of biological chemistry},
  year={1990},
  volume={265 24},
  pages={14234-41}
}
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 (Cys6----Ala), and the recombinant protein was expressed in yeast, purified, characterized for reversible and irreversible denaturation, crystallized isomorphously to the wild-type enzyme, and used to… CONTINUE READING
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