Dynamic force spectroscopy of molecular adhesion bonds.

Phys Rev Lett

Theoretical Molecular Biophysics Group, Max-Planck-Institute for Biophysical Chemistry, 37070 Göttingen, Germany.

Published: June 2000

AI Article Synopsis

  • Recent advancements in techniques like atomic force microscopy and optical tweezers have enhanced the ability to measure molecular responses to mechanical stress.
  • Traditional methods provide limited spatial resolution, capturing only one force value on a force profile that outlines molecular responses along a reaction coordinate.
  • The developed theory enables reconstruction of force profiles from varying loading rates without needing higher resolution, utilizing complementary data from measurements with different spring constants.

Article Abstract

Recent advances in atomic force microscopy, biomembrane force probe experiments, and optical tweezers allow one to measure the response of single molecules to mechanical stress with high precision. Such experiments, due to limited spatial resolution, typically access only one single force value in a continuous force profile that characterizes the molecular response along a reaction coordinate. We develop a theory that allows one to reconstruct force profiles from force spectra obtained from measurements at varying loading rates, without requiring increased resolution. We show that spectra obtained from measurements with different spring constants contain complementary information.

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http://dx.doi.org/10.1103/PhysRevLett.84.6126DOI Listing

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