Theoretical analysis of dynamic force spectroscopy experiments on ligand-receptor complexes.
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 collapse. We conclude that the above mentioned, generally accepted assumption is not satisfied and we discuss possible explanations.
Theoretische Physik, Universität Bielefeld, Universitätsstrasse 25, 33615 Bielefeld, Germany.
M
M
Raible
M
M
Evstigneev
P
P
Reimann
F W
FW
Bartels
R
R
Ros
D001665:Binding Sites; D003198:Computer Simulation; D004247:DNA / Q000032:analysis / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000032:analysis / Q000737:chemistry*; D004548:Elasticity; D008024:Ligands; D046911:Macromolecular Substances / Q000032:analysis / Q000737:chemistry; D008846:Micromanipulation / Q000379:methods*; D018625:Microscopy, Atomic Force / Q000379:methods*; D008956:Models, Chemical; D008967:Molecular Biology / Q000379:methods; D009690:Nucleic Acid Conformation; D010812:Physical Stimulation / Q000295:instrumentation / Q000379:methods; D011485:Protein Binding; D011487:Protein Conformation; D013314:Stress, Mechanical
D004268:DNA-Binding Proteins; D008024:Ligands; D046911:Macromolecular Substances; D004247:DNA