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Crowding-induced stabilization and destabilization in a single protein.

Jordyn M Markle1, Tarynn D Neal1, Hania S Kantzer1

  • 1Department of Chemistry, University of North Carolina at Chapel Hill (UNC-CH), Chapel Hill, North Carolina, USA.

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Summary
This summary is machine-generated.

Cellular protein self-crowding has complex effects on protein stability. Some residues are stabilized, while others are destabilized, revealing the critical role of chemical interactions in crowded biological environments.

Keywords:
NMR spectroscopybiophysicsmacromolecular crowdingprotein foldingprotein–protein interactionsthermodynamics

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Area of Science:

  • Biochemistry
  • Biophysics
  • Molecular Biology

Background:

  • Cellular environments are highly crowded, with protein concentrations reaching up to 300 g/L.
  • Protein crowding significantly impacts protein stability, challenging classic theories that predict only entropy-driven stabilization.
  • Emerging evidence suggests non-covalent chemical interactions play a crucial role in protein stability under crowded conditions.

Purpose of the Study:

  • To investigate the effects of protein self-crowding on stability at the residue level.
  • To explore the mechanisms underlying protein stabilization and destabilization in a physiologically relevant crowded system.
  • To reconcile experimental observations with existing theories of protein crowding.

Main Methods:

  • Utilized Nuclear Magnetic Resonance (NMR)-detected hydrogen-deuterium exchange.
  • Examined the model globular protein GB1 (the B1 domain of streptococcal protein G).
  • Studied protein self-crowding at concentrations up to the solubility limit (100 g/L).

Main Results:

  • Observed differential effects of self-crowding: stabilization of some residues and destabilization of others, contradicting classic theories.
  • Demonstrated that stabilization can be enthalpic, not solely entropic, through temperature-dependence studies.
  • Found that destabilization often increases with concentration, indicating a role for attractive chemical interactions.

Conclusions:

  • Protein self-crowding influences stability through a balance of attractive and repulsive chemical interactions.
  • Repulsive interactions stabilize residues exposed only upon complete unfolding, increasing with protein concentration.
  • Attractive interactions destabilize residues exposed during local unfolding, with destabilization escalating with concentration.