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Related Concept Videos

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Related Experiment Video

Updated: Jun 24, 2026

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope
06:45

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope

Published on: February 28, 2019

Interactions between signal-transducing proteins measured by atomic force microscopy.

Il Hong Kim1, Hye Young Lee, Hae Dong Lee

  • 1National Core Research Center for Systems Bio-Dynamics, Department of Chemistry, Pohang University of Science and Technology, San 31 Hyoja-dong, Pohang, 790-784, Korea.

Analytical Chemistry
|March 28, 2009
PubMed
Summary

Atomic force microscopy (AFM) measured forces between signal proteins. The Phox homology (PX) domain of PLD1 and Src homology (SH3) domain of PLC-gamma1 interact with Munc-18-1, revealing binding dynamics.

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Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
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Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope
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Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
11:13

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

Area of Science:

  • Biophysics
  • Molecular Biology
  • Biochemistry

Background:

  • Signal transduction pathways rely on specific protein-protein interactions.
  • Understanding these interactions at the molecular level is crucial for deciphering cellular mechanisms.

Purpose of the Study:

  • To quantify the specific binding forces between key signal-transducing proteins using Atomic Force Microscopy (AFM).
  • To investigate the dynamics and energy landscape of these biomolecular interactions.

Main Methods:

  • Utilized AFM to measure unbinding forces between immobilized protein domains (PX of PLD1, SH3 of PLC-gamma1) and Munc-18-1.
  • Employed dendron modification on AFM tips and substrates to enhance interaction specificity.
  • Analyzed loading rate dependence of unbinding forces to determine kinetic parameters.

Main Results:

  • Observed single rupture events with unbinding forces of 51 ± 2 pN for PX-(Munc-18-1) and 42 ± 2 pN for PX-SH3.
  • Unbinding forces increased linearly with the logarithm of the loading rate, indicating a single energy barrier.
  • Measured off-rate constants (k(off)) at 15°C were 10⁻³·⁴ ± ⁰·³ s⁻¹ for PX-(Munc-18-1) and 10⁻¹·⁷ ± ⁰·¹ s⁻¹ for PX-SH3.

Conclusions:

  • Quantified the mechanical strength of specific interactions between PLD1-PX, PLC-gamma1-SH3, and Munc-18-1.
  • The observed force-loading rate relationship provides insights into the dissociation energy landscape of these protein interactions.
  • The study elucidates the influence of free interacting partners on binding dynamics.