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Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy
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Ligand-induced structural changes in maltose binding proteins measured by atomic force microscopy.

Cristian Staii1, David W Wood, Giacinto Scoles

  • 1Department of Chemistry, Princeton University, Princeton, New Jersey 08544, USA. cstaii@wisc.edu

Nano Letters
|July 23, 2008
PubMed
Summary

Atomic force microscopy measured the energy of conformational changes in surface-bound maltose binding proteins (MBPs). This study quantizes the energy required for MBP functional transitions, aiding in understanding protein mechanics.

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Area of Science:

  • Biophysics
  • Materials Science
  • Protein Engineering

Background:

  • Maltose binding proteins (MBPs) undergo conformational changes upon ligand binding, crucial for biological function.
  • Understanding these mechanical transitions is key to protein engineering and biomaterials development.

Purpose of the Study:

  • To quantitatively measure the energy associated with the open-closed conformational transition of surface-immobilized dicysteine-terminated maltose binding proteins (dicys-MBPs).
  • To investigate the binding kinetics of different ligands to dicys-MBPs using AFM-based measurements.
  • To validate a mechanical model for surface-immobilized dicys-MBPs.

Main Methods:

  • Utilized atomic force microscopy (AFM) for force-compression measurements on surface-immobilized dicys-MBPs.
  • Employed nanografting to immobilize proteins at defined locations on gold substrates.
  • Performed AFM-friction measurements to compare ligand binding kinetics.

Main Results:

  • Determined the open-closed transition energy for dicys-MBPs to be DeltaE0 = (8 +/- 4) Kcal/mol.
  • Compared binding kinetics for maltose and maltotriose ligands.
  • Results align with a two-lobe model connected by a spring-loaded hinge.

Conclusions:

  • The study provides a quantitative measure of the mechanical energy landscape of MBP conformational changes.
  • AFM force measurements offer insights into protein-ligand interactions and mechanical properties.
  • The findings support a simplified mechanical model for surface-bound MBPs.