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Cold denaturation of proteins.

P L Privalov1

  • 1Institute of Protein Research, Academy of Sciences, Moscow Region, U.S.S.R.

Critical Reviews in Biochemistry and Molecular Biology
|January 1, 1990
PubMed
Summary

Cold denaturation is a common protein unfolding process driven by specific protein-water interactions. This phenomenon challenges traditional views on hydrophobic interactions, highlighting van der Waals forces.

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Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Protein Science

Background:

  • Proteins can unfold at low temperatures (cold denaturation), a phenomenon observed in various globular protein structures.
  • The role of protein hydration and hydrophobic interactions in cold denaturation has been debated.

Purpose of the Study:

  • To summarize experimental evidence on cold denaturation across different protein types.
  • To thermodynamically analyze the causes of cold denaturation.
  • To re-evaluate the mechanism of hydrophobic interactions in light of cold denaturation.

Main Methods:

  • Compilation and analysis of experimental data on protein cold denaturation.
  • Thermodynamic analysis of experimental findings.
  • Calorimetric studies of protein denaturation and non-polar compound transfer.

Main Results:

  • Cold denaturation is a general phenomenon in globular proteins, influenced by urea and guanidine hydrochloride.
  • Protein nonpolar group hydration is thermodynamically favorable and temperature-dependent, driving unfolding at low temperatures.
  • Hydrophobic interactions involve significant van der Waals contributions, revising conventional understanding.

Conclusions:

  • Cold denaturation is a fundamental process governed by specific protein-water interactions.
  • The thermodynamic favorability of hydrating nonpolar groups at low temperatures drives protein unfolding.
  • Hydrophobic interactions are complex, with van der Waals forces playing a key role, not solely hydration effects.

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