Unfolding mechanism of a hyperthermophilic protein O(6)-methylguanine-DNA methyltransferase.

@article{Nishikori2005UnfoldingMO,
  title={Unfolding mechanism of a hyperthermophilic protein O(6)-methylguanine-DNA methyltransferase.},
  author={Shingo Nishikori and Kentaro Shiraki and Shinsuke Fujiwara and Tadayuki Imanaka and Masahiro Takagi},
  journal={Biophysical chemistry},
  year={2005},
  volume={116 2},
  pages={
          97-104
        }
}
Unfolding intermediates have been found only rarely in earlier studies, and how a protein unfolds is therefore poorly understood. In this paper, we show experimental evidence for multiple pathways and multiple intermediates during unfolding reaction of O(6)-methylguanine-DNA methyltransferase from hyperthermophile Thermococcus kodakaraensis (Tk-MGMT). The unfolding profiles monitored by far-UV CD and tryptophan fluorescence were both biphasic, and unfolding monitored by fluorescence was faster… CONTINUE READING
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