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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
The probe is regarded as the heart of any AFM setup and comprises the...

Overview of Microscopy Techniques

Overview of Microscopy Techniques

The early pioneers of microscopy opened a window into the invisible world of microorganisms. In 1830, Joseph Jackson Lister created an essentially modern light microscope. The 20th century saw the development of microscopes that leveraged nonvisible light, such as fluorescence microscopy that uses an ultraviolet light source and electron microscopy that uses short-wavelength electron beams. These advances significantly improved magnification, image resolution, and contrast. By comparison, the...

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Related Experiment Video

Updated: Jun 12, 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

Sampling protein form and function with the atomic force microscope.

Marian Baclayon¹, Wouter H Roos, Gijs J L Wuite

¹Natuur- en Sterrenkunde and Lasercentrum, Vrije Universiteit, Amsterdam, The Netherlands.

Molecular & Cellular Proteomics : MCP

|June 22, 2010

Summary

This summary is machine-generated.

Atomic force microscopy (AFM) images proteins and probes their function in physiological conditions. This technique provides nanoscale insights into protein structure and dynamics, advancing molecular-level biological understanding.

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Last Updated: Jun 12, 2026

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope

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Published on: February 28, 2019

Atomic Force Microscopy of Red-Light Photoreceptors Using PeakForce Quantitative Nanomechanical Property Mapping

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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

Area of Science:

Biophysics
Structural Biology
Proteomics

Background:

Traditional protein analysis often occurs in non-physiological conditions.
Atomic force microscopy (AFM) offers a solution by operating in physiological buffer conditions.

Purpose of the Study:

To review the application of AFM imaging and force spectroscopy in studying protein structure, function, and interactions.
To highlight advances in understanding proteins at the nanoscale within physiologically relevant environments.

Main Methods:

Utilizing atomic force microscopy (AFM) for high-resolution imaging of biological structures without labeling.
Employing AFM in force spectroscopy mode to measure intramolecular interactions and binding strengths.
Following dynamic biological processes in real time under physiological buffer conditions.

Main Results:

AFM enables submolecular resolution imaging of proteins and their conformational changes.
AFM facilitates the mapping of surface proteomes and the study of protein function via force spectroscopy.
The technique bridges research fields by combining protein form and function studies.

Conclusions:

AFM is a powerful biophysical tool for nanoscale analysis of proteins in their native environments.
AFM advances the comprehensive molecular-level understanding of biological processes.
The combined use of AFM imaging and force spectroscopy offers significant insights into protein form and function.