The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: the role of each disulfide bridge.

@article{Yokota2000TheTS,
  title={The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: the role of each disulfide bridge.},
  author={Akiho Yokota and K Izutani and Masayuki Takai and Yoshiyuki Kubo and Yasuo Noda and Yasuko Koumoto and H. Tachibana and Shin-ichi Segawa},
  journal={Journal of molecular biology},
  year={2000},
  volume={295 5},
  pages={1275-88}
}
The effects of lacking a specific disulfide bridge on the transition state in folding were examined in order to explore the folding-unfolding mechanism of lysozyme. Four species of three-disulfide variant of hen lysozyme (3SS-lysozyme) were prepared by replacing two Cys residues with Ala or Ser: C6S/C127A, C30A/C115A, C64A/C80A and C76A/C94A. The recombinant hen lysozyme was studied as the standard reference containing four authentic disulfide bridges and the extra N-terminal Met: the… CONTINUE READING
11 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 11 extracted citations

Similar Papers

Loading similar papers…