Refined procedure of evaluating experimental single-molecule force spectroscopy data.
Dynamic force spectroscopy is a well-established tool to study molecular recognition in a wide range of binding affinities on the single-molecule level. The theoretical interpretation of these data is still very challenging and the models describe the experimental data only partly. In this paper we reconsider the basic assumptions of the models on the basis of an experimental data set and propose an approach of analyzing and quantitatively evaluating dynamic force spectroscopy data on single ligand-receptor complexes. We present our procedure to process and analyze the force-distance curves, to detect the rupture events in an automated manner, and to calculate quantitative parameters for a biophysical characterization of the investigated interaction.
Experimental Biophysics, Physics Department, Bielefeld University, 33615 Bielefeld, Germany.
Alexander
A
Fuhrmann
Dario
D
Anselmetti
Robert
R
Ros
Sebastian
S
Getfert
Peter
P
Reimann
D000465:Algorithms; D001703:Biophysics / Q000379:methods*; D002138:Calibration; D003198:Computer Simulation; D004867:Equipment Design; D008024:Ligands; D019563:Mechanics; D008846:Micromanipulation; D018625:Microscopy, Atomic Force; D008956:Models, Chemical; D008958:Models, Molecular; D008962:Models, Theoretical; D012984:Software; D013053:Spectrophotometry / Q000379:methods*
D008024:Ligands