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Chain Entropy Modulates Cooperativity Selectively within Intermediate Subpopulations during Protein Unfolding.

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Area of Science:

  • Biophysics
  • Protein dynamics
  • Structural biology

Background:

  • Protein unfolding is often cooperative, but the molecular mechanisms driving coordinated structural changes are unclear.
  • Understanding protein dynamics is crucial for deciphering biological function and disease mechanisms.

Purpose of the Study:

  • To investigate the unfolding mechanism of the heterodimeric protein double-chain monellin (dcMN).
  • To elucidate the role of interchain coupling in protein unfolding pathways.
  • To characterize conformational heterogeneity during protein unfolding.

Main Methods:

  • Site-specific time-resolved Förster Resonance Energy Transfer (FRET).
  • Fluorescence anisotropy decay measurements under equilibrium conditions.
  • Maximum entropy method for population-level analysis.

Main Results:

  • Ensemble measurements suggested cooperative unfolding, but population analysis revealed conformational heterogeneity (N-like and U-like subpopulations).
  • Time-resolved anisotropy showed gradual and asynchronous loss of local motional constraints.
  • N-like subpopulations unfolded cooperatively, while U-like subpopulations showed chain-specific, noncooperative unfolding.
  • Covalent linkage of chains suppressed heterogeneity and enforced coordinated unfolding.

Conclusions:

  • Interchain coupling and covalent connectivity restrict chain entropy, influencing unfolding cooperativity.
  • Conformational heterogeneity dictates whether protein unfolding intermediates transition cooperatively or in a chain-specific manner.
  • The study provides molecular insights into the determinants of coordinated protein unfolding.