Unfolding of ribonuclease A on silica nanoparticle surfaces.

@article{Shang2007UnfoldingOR,
  title={Unfolding of ribonuclease A on silica nanoparticle surfaces.},
  author={Wen Shang and Joseph H Nuffer and Jonathan S. Dordick and Richard W. Siegel},
  journal={Nano letters},
  year={2007},
  volume={7 7},
  pages={
          1991-5
        }
}
This paper reports on the unfolding behavior of ribonuclease A (RNase A) on silica nanoparticle surfaces and quantitively demonstrates that nanoscale size and surface curvature play key roles in influencing the stability of adsorbed proteins. Urea denaturation analyses showed that the thermodynamic stability of RNase A decreased upon adsorption onto the nanoparticles, with greater decrease on larger nanoparticles. The stability changes of RNase A correlate well with the changes in the protein… CONTINUE READING

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