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High-Speed Force Spectroscopy for Single Protein Unfolding.

Fidan Sumbul1, Arin Marchesi1, Hirohide Takahashi2

  • 1LAI, Aix-Marseille Université, INSERM UMR_S 1067, CNRS UMR 7333, 13009, Marseille, France.

Methods in Molecular Biology (Clifton, N.J.)
|June 30, 2018
PubMed
Summary

High-speed atomic force microscopy (HS-AFM) enables faster protein unfolding studies. This method provides microsecond resolution for a more complete understanding of protein dynamics and mechanical properties.

Keywords:
Atomic force microscopyCohesionDockerinHigh-speed force spectroscopyProtein unfoldingTitin

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Biochemistry

Background:

  • Single-molecule force spectroscopy (SMFS) quantifies forces for protein domain unfolding.
  • Atomic force microscopy (AFM) is a standard technique for force spectroscopy (FS).
  • Conventional AFM pulling rates offer insights but limit mechanistic exploration.

Purpose of the Study:

  • To present a protocol for high-speed force spectroscopy (HS-FS) using HS-AFM.
  • To achieve microsecond-time resolution for enhanced protein unfolding analysis.
  • To enable comparison between experimental data and simulations.

Main Methods:

  • High-speed atomic force microscopy (HS-AFM) for force spectroscopy.
  • Detailed protocol covering sample preparation, measurements, and data analysis.
  • Application to unfolding of titin I91 domain concatamer.

Main Results:

  • Demonstration of HS-FS protocol for protein unfolding studies.
  • Acquisition of high-resolution data at microsecond timescales.
  • Illustrative example using a well-characterized protein system.

Conclusions:

  • HS-FS significantly advances the study of protein unfolding mechanisms.
  • Microsecond resolution opens new avenues for exploring protein dynamics.
  • The presented protocol facilitates integration of experiments and simulations.