The effect of water on the rate of conformational change in protein allostery.

@article{Goldbeck2001TheEO,
  title={The effect of water on the rate of conformational change in protein allostery.},
  author={Robert A. Goldbeck and Sarah J Paquette and David S Kliger},
  journal={Biophysical journal},
  year={2001},
  volume={81 5},
  pages={
          2919-34
        }
}
The influence of solvation on the rate of quaternary structural change is investigated in human hemoglobin, an allosteric protein in which reduced water activity destabilizes the R state relative to T. Nanosecond absorption spectroscopy of the heme Soret band was used to monitor protein relaxation after photodissociation of aqueous HbCO complex under osmotic stress induced by the nonbinding cosolute poly(ethylene glycol) (PEG). Photolysis data were analyzed globally for six exponential time… CONTINUE READING
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