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Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
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Low temperature protein refolding suggested by molecular simulation.

Daniel J Kozuch1, Frank H Stillinger2, Pablo G Debenedetti1

  • 1Department of Chemical and Biological Engineering, Princeton University, Princeton, New Jersey 08544, USA.

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|November 17, 2019
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Summary

Supercooled water affects protein folding. At very low temperatures, a model protein refolds due to solvent density changes, with implications for cryopreservation and cryomicroscopy.

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Area of Science:

  • Biophysics
  • Physical Chemistry

Background:

  • Protein structure and function are dependent on solvent properties, particularly water.
  • Water exhibits anomalous behavior at supercooled temperatures, influencing biomolecular thermodynamics.

Purpose of the Study:

  • To investigate the impact of supercooled water properties on protein folding thermodynamics.
  • To explore the behavior of a model miniprotein (Trp-cage) at extreme sub-freezing temperatures.

Main Methods:

  • Molecular simulation techniques were employed.
  • The study focused on a model miniprotein, Trp-cage.
  • Simulations were conducted at temperatures as low as 70 K below the solvent's freezing point.

Main Results:

  • Cold denaturation was observed at moderate supercooling.
  • Unexpected cold refolding occurred at deeper supercooling (below 55 K).
  • Refolding is attributed to hydrophobic core desolvation driven by solvent density decrease.

Conclusions:

  • Supercooled water's anomalous properties can induce non-intuitive protein refolding.
  • Findings are relevant to understanding biological processes under cryo-conditions.
  • Implications for cryomicroscopy and cryopreservation techniques.