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Kinetic trapping in protein folding.

Angela E Varela1, Kevin A England1, Silvia Cavagnero1

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Protein folding is often assumed to be thermodynamically controlled, but this review highlights kinetic trapping as crucial. Kinetic trapping protects proteins from aggregation, with cellular machinery clearing any formed aggregates.

Keywords:
kinetic trappingkineticsmetastabilityprotein foldingthermodynamics

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Dynamics

Background:

  • Traditional models propose protein folding is governed by thermodynamics.
  • Anfinsen's principles laid the groundwork for understanding protein folding pathways.
  • However, a broader perspective including aggregates reveals limitations of purely thermodynamic control.

Purpose of the Study:

  • To challenge the assumption of universal thermodynamic control in protein folding.
  • To emphasize the significance of kinetic trapping in protein folding.
  • To explore the protective role of kinetic trapping against protein aggregation.

Main Methods:

  • Review of existing literature on protein folding mechanisms.
  • Analysis of the protein folding landscape including native, unfolded, intermediate, and aggregated states.
  • Theoretical considerations of kinetic trapping and its implications.

Main Results:

  • Protein folding is frequently under kinetic control, not solely thermodynamic control.
  • Kinetic trapping protects the native, bioactive protein state from aggregation.
  • Intracellular disaggregation machines actively manage aberrant protein aggregates.

Conclusions:

  • Kinetic trapping is a vital biological mechanism for maintaining protein function.
  • This mechanism safeguards proteins from potentially harmful aggregation.
  • Cellular systems possess robust mechanisms to reverse aggregation and restore protein bioactivity.