Rough energy landscapes in protein folding: dimeric E. coli Trp repressor folds through three parallel channels.

@article{Gloss2001RoughEL,
  title={Rough energy landscapes in protein folding: dimeric E. coli Trp repressor folds through three parallel channels.},
  author={L. Gloss and B Robert Simler and Charles R. Matthews},
  journal={Journal of molecular biology},
  year={2001},
  volume={312 5},
  pages={1121-34}
}
The folding mechanism of the dimeric Escherichia coli Trp repressor (TR) is a kinetically complex process that involves three distinguishable stages of development. Following the formation of a partially folded, monomeric ensemble of species, within 5 ms, folding to the native dimer is controlled by three kinetic phases. The rate-limiting step in each phase… CONTINUE READING