A common mechanism for recombinant human NGF, BDNF, NT-3, and murine NGF slow unfolding.

@article{Young1999ACM,
  title={A common mechanism for recombinant human NGF, BDNF, NT-3, and murine NGF slow unfolding.},
  author={Linda R De Young and Charles H. Schmelzer and Laureen E. Burton},
  journal={Protein science : a publication of the Protein Society},
  year={1999},
  volume={8 11},
  pages={
          2513-8
        }
}
The recombinant human nerve growth factor (hNGF), brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT-3), neurotrophin 4/5 (NT4/5), and murine NGF (mNGF) dimers all undergo rapid unfolding and dissociation to monomer in GdnHCl. Fluorescence spectroscopy, reversed-phase high-performance liquid chromatography, and size-exclusion chromatography were used to show that this monomer M1 converts slowly to a more fully unfolded monomer, M2, by a first order process with half-lives of 22, 2.5… CONTINUE READING
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