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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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Related Experiment Video

Updated: Sep 30, 2025

Probing the Structure and Dynamics of Interfacial Water with Scanning Tunneling Microscopy and Spectroscopy

Probing the Structure and Dynamics of Interfacial Water with Scanning Tunneling Microscopy and Spectroscopy

Published on: May 27, 2018

Structured Water Molecules on Membrane Proteins Resolved by Atomic Force Microscopy.

Shinichiro Ido¹, Kei Kobayashi¹, Noriaki Oyabu¹

¹Department of Electronic Science and Engineering, Kyoto University, Kyoto-Daigaku-Katsura, Nishikyo, Kyoto, 615-8510, Japan.

|March 11, 2022

Summary

Researchers visualized water molecules near proton pump proteins using 3D force mapping. This technique reveals hydration structures crucial for protein function and applicable to soft nanomaterials.

Keywords:

atomic force microscopy bacteriorhodopsin force mapping hydration protein

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Last Updated: Sep 30, 2025

Probing the Structure and Dynamics of Interfacial Water with Scanning Tunneling Microscopy and Spectroscopy

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Published on: May 27, 2018

Sub-nanometer Resolution Imaging with Amplitude-modulation Atomic Force Microscopy in Liquid

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Published on: December 20, 2016

Atomic Force Microscopy Imaging and Force Spectroscopy of Supported Lipid Bilayers

Atomic Force Microscopy Imaging and Force Spectroscopy of Supported Lipid Bilayers

Published on: July 22, 2015

Area of Science:

Biophysics
Structural Biology
Nanotechnology

Background:

Protein hydration shells are vital for molecular structure and biological activity.
Understanding water structuring at the molecular level is key for biological processes.
Proton pump proteins in purple membranes are essential for cellular energy transduction.

Purpose of the Study:

To measure the molecular-scale hydration structure of native purple membrane patches.
To investigate the role of water in the function of proton pump proteins.
To demonstrate the applicability of a novel imaging technique for soft nanomaterials.

Main Methods:

Utilized frequency modulation atomic force microscopy (FM-AFM).
Employed a noninvasive three-dimensional force mapping technique.
Analyzed native purple membrane patches composed of bacteriorhodopsin.

Main Results:

Successfully resolved ordered water molecules near proton uptake channels of bacteriorhodopsin.
Provided molecular-scale insights into the hydration structure of individual proteins.
Visualized water structuring at the solid-liquid interface.

Conclusions:

The study reveals the precise localization of ordered water molecules in protein hydration shells.
Three-dimensional force mapping is a powerful tool for studying molecular hydration.
This technique has broad applications for investigating soft nanomaterials at the solid-liquid interface.