Structure and hydration of the M-state of the bacteriorhodopsin mutant D96N studied by neutron diffraction.

@article{Weik1998StructureAH,
  title={Structure and hydration of the M-state of the bacteriorhodopsin mutant D96N studied by neutron diffraction.},
  author={Martin Weik and Giuseppe Zaccai and Norbert A. Dencher and Dieter Oesterhelt and Thomas Hau\ss},
  journal={Journal of molecular biology},
  year={1998},
  volume={275 4},
  pages={625-34}
}
Neutron diffraction from oriented purple membrane fragments at various hydration levels, coupled with H2O/2H2O exchange, was used to compare the structure and hydration of the light-adapted initial state (B-state) and the M photointermediate of bacteriorhodopsin mutant D96N. Diffraction patterns were recorded at 86%, 75% and 57% relative humidity (r.h.). Structural changes observed at 86% and 75% r.h. are absent at 57% r.h., showing that they are uncoupled from the deprotonation of the Schiff… CONTINUE READING

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