Preferential interactions of urea with lysozyme and their linkage to protein denaturation.

@article{Timasheff2003PreferentialIO,
  title={Preferential interactions of urea with lysozyme and their linkage to protein denaturation.},
  author={Serge N Timasheff and Guifu Xie},
  journal={Biophysical chemistry},
  year={2003},
  volume={105 2-3},
  pages={421-48}
}
The interactions involved in the denaturation of lysozyme in the presence of urea were examined by thermal transition studies and measurements of preferential interactions of urea with the protein at pH 7.0, where it remains native up to 9.3 M urea, and at pH 2.0, where it undergoes a transition between 2.5 and 5.0 M urea. The destabilization of lysozyme by urea was found to follow the linear dependence on urea molar concentration, M(u), DeltaG(u)(o)=DeltaG(w)(o)-2.1 M(u), over the combined… CONTINUE READING