Conformational substates and motions in myoglobin. External influences on structure and dynamics.

@article{Hong1990ConformationalSA,
  title={Conformational substates and motions in myoglobin. External influences on structure and dynamics.},
  author={Myung Ki Hong and Daniel N. Braunstein and B. R. Cowen and Hans Frauenfelder and Jr Icko Iben and Judith Renee Mourant and P{\'a}l Ormos and Reinhard Scholl and Alexandra Schulte and Peter J. Steinbach},
  journal={Biophysical journal},
  year={1990},
  volume={58 2},
  pages={
          429-36
        }
}
Myoglobin, a simppe dioxygen-storage protein, is a good laboratory for the investigation of the connection between protein structure, dynamics, and function. Fourier-transform infrared spectroscopy on carbon-monoxymyoglobin (MbCO) shows three major CO bands. These bands are excellent probes for the investigation of the structure-function relationship. They have different CO binding kinetics and their CO dipoles form different angles with respect to the heme normal, implying that MbCO exists in… CONTINUE READING

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