Calorimetric studies of the kinetic unfreezing of molecular motions in hydrated lysozyme, hemoglobin, and myoglobin.

@article{Sartor1994CalorimetricSO,
  title={Calorimetric studies of the kinetic unfreezing of molecular motions in hydrated lysozyme, hemoglobin, and myoglobin.},
  author={Giovanni Sartor and Erwin Mayer and G P Johari},
  journal={Biophysical journal},
  year={1994},
  volume={66 1},
  pages={
          249-58
        }
}
Differential scanning calorimetric (DSC) studies of the glassy states of as-received and hydrated lysozyme, hemoglobin, and myoglobin powders, with water contents of < or = 0.25, < or = 0.30, and < or = 0.29 g/g of protein, show that their heat capacity slowly increases with increasing temperature, without showing an abrupt increase characteristic of glass-->liquid transition. Annealing (also referred to as physical aging) of the hydrated proteins causes their DSC scans to show an endothermic… CONTINUE READING

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