Effect of hydrostatic pressure on unfolding of alpha-lactalbumin: volumetric equivalence of the molten globule and unfolded state.

@article{Kobashigawa1999EffectOH,
  title={Effect of hydrostatic pressure on unfolding of alpha-lactalbumin: volumetric equivalence of the molten globule and unfolded state.},
  author={Yoshihiro Kobashigawa and Minoru Sakurai and Katsutoshi Nitta},
  journal={Protein science : a publication of the Protein Society},
  year={1999},
  volume={8 12},
  pages={2765-72}
}
The effect of pressure on the unfolding of bovine alpha-lactalbumin was investigated by ultraviolet absorption methods. The change of molar volume associated with unfolding, deltaV, was measured in the presence or absence of guanidine hydrochloride at pH 7. The deltaV was estimated to be -63 cm3/mol in the absence of a chemical denaturant. While in the presence of guanidine hydrochloride (GuHCl), it was found that deltaV was -66 cm3/mol at 25 degrees C and was independent of the concentration… CONTINUE READING