Thermal unfolding of proteins at high pH range studied by UV absorbance.

@article{Melo1997ThermalUO,
  title={Thermal unfolding of proteins at high pH range studied by UV absorbance.},
  author={Eduardo Pinho e Melo and Maria Raquel Aires-Barros and S{\'i}lvia M. B. Costa and Joaquim Manuel Sampaio Cabral},
  journal={Journal of biochemical and biophysical methods},
  year={1997},
  volume={34 1},
  pages={45-59}
}
This work describes a methodology to monitor protein unfolding by using the well known changes in tyrosine absorbance with the ionization of the side chain phenol group. It can be applied to proteins that are functionally active at pH values higher than 9.0 where the current UV differential spectroscopy technique can not be used. The simplicity and facility of the proposed methodology (only two absorbance measurements have to be acquired) can make it very useful namely for technological… CONTINUE READING

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