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Related Concept Videos

Mechanical Protein Functions01:58

Mechanical Protein Functions

Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
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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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Forcing a Molecule to Switch: Quantifying Mechanical Control at the Atomic Scale.

A M Shashika D Wijerathna1, Markus Zirnheld1, Michael L Hildebrand1

  • 1Department of Physics, Old Dominion University, Norfolk, Virginia 23529, United States.

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Researchers quantified the forces driving single-molecule conformational changes using atomic force microscopy. They found long-range interactions mechanically deform molecules, enabling switching through a deformation-assisted pathway.

Keywords:
conformational molecular switchqPlus atomic force microscopyscanning tunneling microscopysingle-molecule force spectroscopy

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Area of Science:

  • Surface Science
  • Chemical Physics
  • Nanotechnology

Background:

  • Single-molecule mechanical switching is key to molecular function.
  • Quantitative force and energy landscape data for these transitions are scarce.
  • Understanding these forces is crucial for molecular control.

Purpose of the Study:

  • To quantitatively characterize the force and energy landscape of mechanically induced conformational switching.
  • To investigate the role of intermolecular forces in molecular deformation and switching.
  • To establish a framework for controlling single-molecule mechanical functionality.

Main Methods:

  • Utilized qPlus atomic force microscopy (AFM) to probe individual TBrPP-Co(II) molecules on Au(111).
  • Reconstructed interaction potentials from 3D force-distance data (Δf(x,y,z)).
  • Employed the inflection point test for validation of measurement reliability.

Main Results:

  • Determined a threshold force of approximately 96 ± 8 pN for conformational switching.
  • Quantified the tip-induced switching interaction energy at approximately 38 ± 4 meV.
  • Observed a power-law force dependence (exponent ~6) at longer distances, indicating van der Waals interactions, with deviations at closer distances revealing deformation.

Conclusions:

  • Long-range dispersive interactions can mechanically deform molecules, facilitating conformational switching via a deformation-assisted pathway.
  • Provided a quantitative understanding of the forces governing single-molecule mechanical transitions.
  • Established a foundation for precise control over mechanically driven molecular functionality.