Regensburg 2007 – wissenschaftliches Programm
Bereiche | Tage | Auswahl | Suche | Downloads | Hilfe
BP: Fachverband Biologische Physik
BP 26: Poster Session II
BP 26.29: Poster
Donnerstag, 29. März 2007, 17:00–19:30, Poster B
Improved data analysis for single molecule force spectroscopy experiments — •Alexander Fuhrmann1, Sebastian Getfert2, Dario Anselmetti1, Peter Reimann2, and Robert Ros1 — 1Experimental Biophysics — 2Condensed Matter Theory, Physics Department, Bielefeld University, 33615 Bielefeld, Germany
Dynamic force spectroscopy (DFS) is widely used to investigate ligand-receptor interactions on the single molecule level. However, the data analysis is still a challenging task. The framework of the standard theory by Evans and Ritchie [1] has been extended by Raible et al. [2] in order to consistently describe the experimental data by taking into account heterogeneity of chemical bonds via random variations of the force-dependent dissociation rate. An important implication of these theories is that during pulling of the molecules all elastic components must be in equilibrium. Accordingly the force-extension curves before the dissociation of the ligand-receptor complexes must follow a distinct master curve, independently of the particular pulling velocity. Here, we present an analysis method based on the construction of master curves, which significantly increases the consistence of our experimental data with the model of chemical bond heterogeneity. Additionally, analysing the molecular elasticity in relation to the dissociation forces in 2D-histogramms allows a qualitative identification of different binding modes.
[1] E. Evans and K. Ritchie; Biophys.J. 72:1541 (1997) [2] M. Raible, M. Evstigneev, F. W. Bartels, R. Eckel, M. Nguyen-Duong, R. Merkel, R. Ros, D. Anselmetti, and P. Reimann; Biophys.J. 90: 3851 (2006).