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A Protocol for Using Förster Resonance Energy Transfer (FRET)-force Biosensors to Measure Mechanical Forces across the Nuclear LINC Complex
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Direction-dependent mechanical unfolding and green fluorescent protein as a force sensor.

M Caraglio1, A Imparato, A Pelizzola

  • 1Dipartimento di Fisica and CNISM, Politecnico di Torino, c. Duca degli Abruzzi 24, Torino, Italy. michele.caraglio@polito.itv

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
|September 21, 2011
PubMed
Summary

We modeled protein mechanical unfolding using an Ising-like approach. Varying pulling direction accurately predicted unfolding forces and revealed pathways, leading to a novel force sensor design.

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Last Updated: May 29, 2026

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09:43

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Published on: April 11, 2017

Measurement of Force-Sensitive Protein Dynamics in Living Cells Using a Combination of Fluorescent Techniques
08:28

Measurement of Force-Sensitive Protein Dynamics in Living Cells Using a Combination of Fluorescent Techniques

Published on: November 2, 2018

Area of Science:

  • Biophysics
  • Computational Biology
  • Protein Dynamics

Background:

  • Understanding protein mechanical unfolding is crucial for molecular biology.
  • Experimental studies observe distinct unfolding pathways and forces.
  • Computational models are needed to simulate and predict these behaviors.

Purpose of the Study:

  • To investigate the mechanical unfolding of green fluorescent protein (GFP) using an Ising-like model.
  • To explore how different pulling directions affect unfolding pathways and forces.
  • To propose a novel force sensor based on mechanical unfolding properties.

Main Methods:

  • Utilized an Ising-like model for protein simulation.
  • Simulated mechanical unfolding of GFP under directional pulling.
  • Analyzed unfolding pathways and calculated unfolding forces.

Main Results:

  • The model reproduced experimentally observed major and minor unfolding pathways of GFP when pulled from its ends.
  • Varying the pulling direction yielded accurate magnitudes and rankings of unfolding forces.
  • Direction-dependent unfolding forces at equilibrium were identified.

Conclusions:

  • The Ising-like model effectively captures protein mechanical unfolding dynamics.
  • Pulling direction is a critical factor influencing protein mechanical stability.
  • A new force sensor concept leveraging directional unfolding forces was proposed.