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Related Experiment Video

Updated: May 24, 2026

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope
06:45

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope

Published on: February 28, 2019

Physical microscopic model of proteins under force.

Nikolay V Dokholyan1

  • 1Department of Biochemistry and Biophysics, University of North Carolina, School of Medicine, Chapel Hill, North Carolina 27599, USA. dokh@unc.edu

The Journal of Physical Chemistry. B
|March 2, 2012
PubMed
Summary

Nature

Area of Science:

  • Biophysics
  • Molecular Biology
  • Protein Mechanics

Background:

  • Proteins in living cells are evolved to sense and counteract mechanical forces.
  • Multidomain proteins achieve high sensitivity and dynamic range through complex structures.
  • Individual domains and linking peptides contribute to protein force response.

Purpose of the Study:

  • To model and understand the force response of individual protein domains.
  • To investigate the mechanical behavior of multidomain proteins under force.
  • To establish a framework for interpreting force-based experiments on proteins.

Main Methods:

  • Utilized a simplified protein model for computational analysis.
  • Analyzed the force-dependent extension of individual domains.

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  • Examined the collective force response of multidomain protein structures.

    • Main Results:

    • Individual domain extension scales linearly with applied force.
    • Multidomain protein response is dictated by linking peptides at low force and domain unfolding at high force.
    • Force-extension curves exhibit multiple sigmoidal transitions.

    Conclusions:

    • Protein force response is a composite behavior arising from its constituent domains and linkers.
    • The study provides a foundational model for understanding protein mechanics.
    • This framework aids in interpreting experimental data from force spectroscopy.