Osmolyte-induced folding of an intrinsically disordered protein: folding mechanism in the absence of ligand.

@article{Chang2010OsmolyteinducedFO,
  title={Osmolyte-induced folding of an intrinsically disordered protein: folding mechanism in the absence of ligand.},
  author={Yu-Chu Chang and Terrence G. Oas},
  journal={Biochemistry},
  year={2010},
  volume={49 25},
  pages={5086-96}
}
Understanding the interconversion between thermodynamically distinguishable states present in a protein folding pathway provides not only the kinetics and energetics of protein folding but also insights into the functional roles of these states in biological systems. The protein component of the bacterial RNase P holoenzyme from Bacillus subtilis (P protein) was previously shown to be unfolded in the absence of its cognate RNA or other anionic ligands. P protein was used in this study as a… CONTINUE READING
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2007)Application of the TransferModel to Understand How Naturally Occurring Osmolytes Affect Protein Stability

  • M. Auton, D. andBolen
  • Methods Enzymol
  • 2007

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