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Related Experiment Video

Updated: Jul 14, 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

Exploring the molecular forces within and between CbsA S-layer proteins using single molecule force spectroscopy.

Claire Verbelen¹, Jenni Antikainen, Timo K Korhonen

¹Unité de chimie des interfaces, Université catholique de Louvain, Croix du Sud 2/18, B-1348 Louvain-la-Neuve, Belgium.

Ultramicroscopy

|June 15, 2007

Summary

Single molecule atomic force microscopy revealed the forces behind S-layer protein CbsA folding and assembly. Unfolding alpha-helices and intermolecular forces were quantified, providing insights into protein stability.

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Last Updated: Jul 14, 2026

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope

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Published on: February 28, 2019

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Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

Area of Science:

Biophysics
Protein Science
Microscopy

Background:

S-layer proteins form a crystalline outer layer in many bacteria.
Understanding the molecular forces of S-layer protein assembly is crucial for biotechnological applications.

Purpose of the Study:

To investigate the intra- and intermolecular forces governing the folding and assembly of the S-layer protein CbsA using atomic force microscopy.

Main Methods:

Single molecule atomic force microscopy (AFM) was employed to measure forces between CbsA proteins.
Force curves were analyzed to identify unfolding events and intermolecular interactions.

Main Results:

Sawtooth patterns in force curves indicated alpha-helix unfolding (58+/-26pN).
Truncated CbsA peptides showed increased domain stability (83+/-45pN).
Cationic N-terminal peptides exhibited strong intermolecular forces (366+/-149pN), dependent on pulling speed and interaction time.

Conclusions:

Measured intra- and intermolecular forces are critical for CbsA protein stability and assembly.
AFM provides valuable insights into the mechanical properties of S-layer proteins.
These findings have implications for understanding bacterial cell surface organization and protein engineering.