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Crowding and Confinement Can Oppositely Affect Protein Stability.

Kai Cheng1, Qiong Wu1, Zeting Zhang1

  • 1Key Laboratory of Magnetic Resonance in Biological Systems State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan Collaborative Innovation Center of Chemistry for Life Sciences, Wuhan, Institute of Physics and Mathematics Chinese Academy of Sciences, Wuhan, 430071, P. R. China.

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Cellular environments affect protein stability. This study quantifies how crowding stabilizes proteins, while confinement destabilizes them, highlighting the crucial role of chemical interactions in protein folding.

Keywords:
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Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Molecular Biology

Background:

  • Cellular environments are crowded and confined, influencing protein behavior.
  • Simple theories predict entropic stabilization of proteins in these conditions.
  • However, chemical interactions also play a significant role, necessitating quantitative studies.

Purpose of the Study:

  • To quantitatively assess the impact of crowding and confinement on protein unfolding thermodynamics.
  • To investigate the balance between hard-core repulsions and chemical interactions in protein stability.
  • To compare the effects of monomers versus polymers as crowding agents.

Main Methods:

  • Utilized a model globular protein (KH1) for experiments.
  • Quantified equilibrium unfolding thermodynamics.
  • Employed synthetic-polymer crowding agents and reverse micelles for confinement studies.

Main Results:

  • Protein KH1 was stabilized by synthetic-polymer crowding agents.
  • Confinement in reverse micelles destabilized KH1.
  • Monomer solutions showed greater entropic stabilization and enthalpic destabilization than polymer solutions.
  • Confinement decreased the temperature of maximum stability and melting temperature, with entropic destabilization and enthalpic stabilization.

Conclusions:

  • Results challenge simple theoretical predictions, emphasizing the importance of chemical interactions.
  • Crowding and confinement exert distinct, complex effects on protein folding thermodynamics.
  • Cells likely leverage chemical interactions to fine-tune protein stability in vivo.