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Protein Folding

Protein Folding

Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Atomic Force Microscopy

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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.
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Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Updated: May 29, 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

Single-molecule protein unfolding and refolding using atomic force microscopy.

Thomas Bornschlögl¹, Matthias Rief

¹Department of Physics, TU Munich, Garching, Germany.

Methods in Molecular Biology (Clifton, N.J.)

|September 13, 2011

Summary

This summary is machine-generated.

Atomic force microscopy (AFM) enables single-molecule mechanical studies of protein unfolding and refolding. This guide provides protocols for producing protein chains and analyzing AFM data, including techniques for low-force measurements.

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Area of Science:

Biophysics
Molecular Biology
Nanotechnology

Background:

Atomic force microscopy (AFM) is a key tool for single-molecule mechanical analysis of proteins.
AFM complements other single-molecule techniques for studying protein folding and unfolding.
Many proteins function under mechanical stress, making AFM crucial for physiological studies.

Purpose of the Study:

To provide protocol-like instructions for researchers new to AFM for studying protein unfolding and refolding.
To detail methods for producing polyproteins or modular protein chains for AFM experiments.
To explain basic AFM data collection and analysis, including techniques for low-force measurements.

Main Methods:

Production of polyproteins or modular protein chains.
Data collection using atomic force microscopy (AFM).
Basic data analysis and averaging techniques for enhanced force resolution.

Main Results:

Established protocols for preparing protein samples for AFM.
Demonstrated methods for collecting and analyzing single-molecule mechanical unfolding data.
Introduced an averaging technique to improve force resolution for low-force protein unfolding/folding.

Conclusions:

AFM is a powerful technique for investigating protein mechanics at the single-molecule level.
This guide facilitates the application of AFM for studying protein unfolding and refolding.
The described methods enhance the ability to study proteins under physiologically relevant mechanical forces.