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Correlations within polyprotein forced unfolding dwell-times introduce sequential dependency.

Einat Chetrit1, Yasmine Meroz2, Ziv Klausner3

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Summary

Mechanical forces cause polyproteins to unfold, but their unfolding times are not independent. This study reveals correlated unfolding behaviors in polyproteins, challenging previous assumptions and offering new insights into their elasticity.

Keywords:
AFMCorrelationsForce-spectroscopyNon-exponential kineticsPolyproteinSingle-molecule

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Area of Science:

  • Biophysics
  • Materials Science
  • Molecular Biology

Background:

  • Polyproteins unfold and extend under mechanical load, a process crucial for their function and elasticity.
  • The arrangement of proteins and linkers dictates polyprotein performance.
  • Unfolding times are often assumed to be independent and identically distributed (exponentially distributed).

Purpose of the Study:

  • To investigate the unfolding kinetics of polyproteins using single molecule force spectroscopy (SMFS).
  • To analyze the statistical distribution of unfolding time-intervals in polyproteins.
  • To provide a physical explanation for non-exponential unfolding time distributions observed in polyproteins.

Main Methods:

  • Utilized SMFS with Atomic Force Microscopy (AFM) to measure unfolding kinetics.
  • Applied three statistical analysis approaches to unfolding time-intervals.
  • Employed continuous time random walk (CTRW) and free-energy reconstruction.

Main Results:

  • Observed an 'N-effect,' indicating hierarchical behavior and non-identical unfolding time distributions.
  • Unfolding times exhibited subdiffusive features as analyzed by CTRW.
  • Demonstrated that the elongating polypeptide chain influences sequential unfolding probabilities.

Conclusions:

  • Polyprotein unfolding kinetics deviate from the assumption of independent and identically distributed unfolding times.
  • The physical mechanism involves correlations introduced by the elongating polypeptide chain.
  • Findings offer a deeper understanding of polyprotein mechanics and elasticity regulation.