The forced rupture of single chemical bonds in biomolecular compounds (e.g. ligand–receptor systems) as observed in dynamic force spectroscopy experiments is addressed. Under the assumption that the probability of bond rupture depends only on the instantaneously acting force, a data collapse onto a single master curve is predicted. For rupture data obtained experimentally by dynamic AFM force spectroscopy of a ligand–receptor bond between a DNA and a regulatory protein we do not find such a col-lapse. We conclude that the above mentioned, generally accepted assumption is not satisfied and we discuss possible explanations
We probe the dynamic strength of multiple biotin-streptavidin adhesion bonds under linear loading us...
none1noTraditionally, protein-protein adhesion interactions have been studied in reversible equilibr...
Force spectroscopy measurements of the rupture of the molecular bond between biotin and streptavidin...
Raible M, Evstigneev M, Reimann P, Bartels FW, Ros R. Theoretical analysis of dynamic force spectros...
AbstractIn dynamic force spectroscopy, a (bio-)molecular complex is subjected to a steadily increasi...
AbstractIn dynamic force spectroscopy, a (bio-)molecular complex is subjected to a steadily increasi...
Getfert S, Reimann P. Hidden Multiple Bond Effects in Dynamic Force Spectroscopy. Biophysical Journa...
Fuhrmann A, Anselmetti D, Ros R, Getfert S, Reimann P. Refined procedure of evaluating experimental ...
Dynamic force spectroscopy (DFS) makes it possible to investigate specific interactions between two ...
Dynamic force spectroscopy (DFS) makes it possible to investigate specific interactions between two ...
Atomic force microscope based single-molecule force spectroscopy provides a description of a variety...
AbstractSmall ligands and their receptors are widely used non-covalent couplers in various biotech a...
International audienceDynamic force spectroscopy (DFS), using atomic force microscopy (AFM), is a po...
Dynamic force spectroscopy probes the kinetic and thermodynamic properties of single molecules and m...
AbstractSingle-molecule force spectroscopy is used to probe the kinetics of receptor-ligand bonds by...
We probe the dynamic strength of multiple biotin-streptavidin adhesion bonds under linear loading us...
none1noTraditionally, protein-protein adhesion interactions have been studied in reversible equilibr...
Force spectroscopy measurements of the rupture of the molecular bond between biotin and streptavidin...
Raible M, Evstigneev M, Reimann P, Bartels FW, Ros R. Theoretical analysis of dynamic force spectros...
AbstractIn dynamic force spectroscopy, a (bio-)molecular complex is subjected to a steadily increasi...
AbstractIn dynamic force spectroscopy, a (bio-)molecular complex is subjected to a steadily increasi...
Getfert S, Reimann P. Hidden Multiple Bond Effects in Dynamic Force Spectroscopy. Biophysical Journa...
Fuhrmann A, Anselmetti D, Ros R, Getfert S, Reimann P. Refined procedure of evaluating experimental ...
Dynamic force spectroscopy (DFS) makes it possible to investigate specific interactions between two ...
Dynamic force spectroscopy (DFS) makes it possible to investigate specific interactions between two ...
Atomic force microscope based single-molecule force spectroscopy provides a description of a variety...
AbstractSmall ligands and their receptors are widely used non-covalent couplers in various biotech a...
International audienceDynamic force spectroscopy (DFS), using atomic force microscopy (AFM), is a po...
Dynamic force spectroscopy probes the kinetic and thermodynamic properties of single molecules and m...
AbstractSingle-molecule force spectroscopy is used to probe the kinetics of receptor-ligand bonds by...
We probe the dynamic strength of multiple biotin-streptavidin adhesion bonds under linear loading us...
none1noTraditionally, protein-protein adhesion interactions have been studied in reversible equilibr...
Force spectroscopy measurements of the rupture of the molecular bond between biotin and streptavidin...