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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...

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Updated: Apr 30, 2026

Visualization of Recombinant DNA and Protein Complexes Using Atomic Force Microscopy

Visualization of Recombinant DNA and Protein Complexes Using Atomic Force Microscopy

Published on: July 18, 2011

Localizing chemical groups while imaging single native proteins by high-resolution atomic force microscopy.

Moritz Pfreundschuh¹, David Alsteens, Manuel Hilbert

¹Department of Biosystems Science and Engineering, ETH Zurich , Mattenstrasse 26, 4058 Basel, Switzerland.

|April 29, 2014

Summary

This summary is machine-generated.

This study introduces a novel atomic force microscopy (AFM) technique for high-resolution protein imaging. The method precisely maps chemical interaction sites, like histidine residues, on single proteins, advancing biophysical and nanotechnological applications.

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Area of Science:

Biophysics
Biochemistry
Nanotechnology

Background:

Mapping chemical interaction sites on proteins is crucial for understanding protein behavior and biotechnological applications.
Current methods face challenges in achieving simultaneous high-resolution imaging and localization of these sites on native proteins.

Purpose of the Study:

To develop and demonstrate a novel method for high-resolution imaging and localization of chemical interaction sites on single native proteins.
To characterize the self-assembly of SAS-6 protein and map its interaction sites.

Main Methods:

Utilized force-distance curve-based atomic force microscopy (FD-based AFM).
Employed AFM tips functionalized with Ni(2+)-N-nitrilotriacetate (Ni(2+)-NTA) groups.
Applied the technique to image SAS-6 protein and map histidine residues.

Main Results:

Achieved high-resolution imaging of SAS-6 protein structures.
Successfully located specific interaction sites on SAS-6 at nanometer resolution.
Quantified the binding strength between Ni(2+)-NTA groups and histidine residues.

Conclusions:

FD-based AFM is a powerful tool for structural mapping and characterization of protein interaction sites.
The developed surface chemistry can be adapted to map various chemical sites on proteins.
This technique offers broad applicability for studying native proteins in biophysical and nanotechnological research.