The unfolding mechanism and the disulfide structures of denatured lysozyme.

@article{Chang2002TheUM,
  title={The unfolding mechanism and the disulfide structures of denatured lysozyme.},
  author={J Y Chang and Li Ken Li},
  journal={FEBS letters},
  year={2002},
  volume={511 1-3},
  pages={73-8}
}
The mechanism of denaturation and unfolding of lysozyme has been characterized here using the method of disulfide scrambling. Under denaturing conditions (urea, guanidinium hydrochloride (GdmCl), guanidinium thiocyanate (GdmSCN), or elevated temperature) and in the presence of thiol initiator, lysozyme denatures by shuffling its four native disulfide bonds and converts to a mixture of fully oxidized scrambled isomers. To denature 50% of the native lysozyme requires 1.1 M of GdmSCN, 2.8 M of… CONTINUE READING

From This Paper

Topics from this paper.
14 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 14 extracted citations

Similar Papers

Loading similar papers…