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Atomic Force Microscopy

Atomic Force Microscopy

Atomic force microscopy (AFM) is a type of scanning probe microscopy that can analyze topographic details of various specimens like ceramics, glass, polymers, and biological samples. AFM offers over 1000 times more resolution than the optical imaging system. Images generated from AFM are three-dimensional surface profiles, offering an advantage over the flat, two-dimensional images from other imaging techniques.
The AFM Probe
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Updated: Mar 30, 2026

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope

Published on: February 28, 2019

On artifacts in single-molecule force spectroscopy.

Pilar Cossio¹, Gerhard Hummer¹, Attila Szabo²

¹Department of Theoretical Biophysics, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany; pilar.cossio@biophys.mpg.de gerhard.hummer@biophys.mpg.de attilas@nih.gov.

Proceedings of the National Academy of Sciences of the United States of America

|November 6, 2015

Summary

This summary is machine-generated.

This study analyzes how linker and pulling device dynamics affect biomolecule conformational transitions in force spectroscopy. It corrects for artifacts, improving the accuracy of force-clamp and force-ramp experiments.

Keywords:

anisotropic diffusion free energy surface pulling device unfolding rate

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Last Updated: Mar 30, 2026

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Area of Science:

Biophysics
Polymer Physics

Background:

Force spectroscopy uses polymer linkers to probe biomolecule conformational changes.
Extracting transition rates can be complicated by experimental setup dynamics.

Purpose of the Study:

To investigate the influence of linker and pulling device dynamics on conformational transition rates.
To develop analytic expressions for observables in force-clamp and force-ramp experiments.
To identify and correct for artifacts in force spectroscopy data analysis.

Main Methods:

Derivation of analytic expressions for observables.
Analysis of force-clamp and force-ramp experimental data.
Theoretical modeling of linker and pulling device dynamics.

Main Results:

Identified artifacts arising from slow linker/device dynamics and high-force linker stretching.
Derived expressions accounting for mechanical response and dynamics.
Found a linker and loading rate-dependent correction for force-ramp experiments.

Conclusions:

The developed theory provides a framework for designing and analyzing force spectroscopy experiments.
Highlights and corrects for factors complicating the interpretation of transition rates.
Improves quantitative analysis of biomolecular force spectroscopy data.