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Single polyprotein unfolding shows history dependence, with increasing forces and decreasing stiffness in consecutive events. This challenges prior models, revealing viscoelastic linker properties and force-rate kinetics govern unfolding dynamics.

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Area of Science:

  • Biophysics
  • Polymer Physics
  • Molecular Biology

Background:

  • Polyproteins are macromolecules with tandem folded domains and linkers.
  • Biological stresses can induce partial unfolding and extension in polyproteins.
  • Previous studies suggested history dependence in polyprotein forced unfolding.

Purpose of the Study:

  • To investigate the unfolding behavior of single poly(I91) octamers.
  • To understand the hierarchy and mechanical properties during sequential unfolding events.
  • To elucidate the role of viscoelasticity and force-rate in polyprotein unfolding.

Main Methods:

  • Single-molecule force spectroscopy on poly(I91) octamers.
  • Brownian dynamics simulations.
  • Mechanistic viscoelastic modeling.

Main Results:

  • Observed an increasing hierarchy in unfolding forces during sequential events.
  • Measured a decrease in effective stiffness with consecutive unfolding.
  • Demonstrated that linker viscoelasticity and force-rate application govern unfolding kinetics.

Conclusions:

  • Polyprotein unfolding exhibits history dependence, contrary to expectations of independent events.
  • Viscoelastic properties of the growing linker chain create unfolding hierarchies.
  • Force-rate application is a critical factor in polyprotein unfolding kinetics.