Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR.

@article{Uzawa2008HierarchicalFM,
  title={Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR.},
  author={Takanori Uzawa and Chiaki Nishimura and Shuji Akiyama and Koichiro Ishimori and Satoshi Takahashi and H Jane Dyson and Peter E. Wright},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2008},
  volume={105 37},
  pages={13859-64}
}
The earliest steps in the folding of proteins are complete on an extremely rapid time scale that is difficult to access experimentally. We have used rapid-mixing quench-flow methods to extend the time resolution of folding studies on apomyoglobin and elucidate the structural and dynamic features of members of the ensemble of intermediate states that are populated on a submillisecond time scale during this process. The picture that emerges is of a continuum of rapidly interconverting states… CONTINUE READING