Hydrodynamic effects in fast AFM single-molecule force measurements

@article{Janovjak2004HydrodynamicEI,
  title={Hydrodynamic effects in fast AFM single-molecule force measurements},
  author={Harald Janovjak and Jens Struckmeier and Daniel J M{\"u}ller},
  journal={European Biophysics Journal},
  year={2004},
  volume={34},
  pages={91-96}
}
Atomic force microscopy (AFM) allows the critical forces that unfold single proteins and rupture individual receptor–ligand bonds to be measured. To derive the shape of the energy landscape, the dynamic strength of the system is probed at different force loading rates. This is usually achieved by varying the pulling speed between a few nm/s and a few μm/s, although for a more complete investigation of the kinetic properties higher speeds are desirable. Above 10 μm/s, the hydrodynamic drag force… CONTINUE READING