Protein flexibility and conformational state: a comparison of collective vibrational modes of wild-type and D96N bacteriorhodopsin.

@article{Whitmire2003ProteinFA,
  title={Protein flexibility and conformational state: a comparison of collective vibrational modes of wild-type and D96N bacteriorhodopsin.},
  author={Scott Whitmire and Daniel Wolpert and Andrea G. Markelz and Jason R. Hillebrecht and Jhenny Flor Galan and Robert R. Birge},
  journal={Biophysical journal},
  year={2003},
  volume={85 2},
  pages={1269-77}
}
Far infrared (FIR) spectral measurements of wild-type (WT) and D96N mutant bacteriorhodopsin thin films have been carried out using terahertz time domain spectroscopy as a function of hydration, temperature, and conformational state. The results are compared to calculated spectra generated via normal mode analyses using CHARMM. We find that the FIR absorbance is slowly increasing with frequency and without strong narrow features over the range of 2-60 cm(-1) and up to a resolution of 0.17 cm(-1… CONTINUE READING
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