Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studies.

@article{Chen1989LowtemperatureUO,
  title={Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studies.},
  author={Buo Chen and John A. Schellman},
  journal={Biochemistry},
  year={1989},
  volume={28 2},
  pages={685-91}
}
The mutant protein I3C-C97/C54T of phage T4 lysozyme is free of sulfhydryl groups and has a genetically engineered disulfide bridge between positions 3 and 97 (Perry & Wetzel, 1986). This protein has a maximum stability at 12 degrees C in 3 M guanidinium chloride and undergoes reversible high- and low-temperature melting at 28 and -3 degrees C, respectively, in this medium. The free energy of stabilization of the protein has been studied over a range of temperature that includes both melting… CONTINUE READING