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Updated: Jun 20, 2026

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope
Published on: February 28, 2019
The effect of different force applications on the protein-protein complex Barnase-Barstar
Jan Neumann1, Kay-Eberhard Gottschalk
1Angewandte Physik und Biophysik, Ludwig-Maximilians Universität, Munich, Germany.
Abstract:
Steered molecular dynamics simulations are a tool to examine the energy landscape of protein-protein complexes by applying external forces. Here, we analyze the influence of the velocity and geometry of the probing forces on a protein complex using this tool. With steered molecular dynamics, we probe the stability of the protein-protein complex Barnase-Barstar. The individual proteins are mechanically labile. The Barnase-Barstar binding site is more stable than the folds of the individual proteins. By using different force protocols, we observe a variety of responses of the system to the applied tension.
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