Unknown

Dataset Information

0

Two barriers or not? Dynamic force spectroscopy on the integrin ?7?1 invasin complex.


ABSTRACT: Dynamic force spectroscopy was used to test force-induced dissociation of the complex between the integrin ?7?1 and the bacterial protein invasin. Both proteins were used in truncated forms comprising the respective binding sites. Using the biomembrane force-probe, the bond system was exposed to 14 different loading rates ranging from 18 pN/s to 5.3 nN/s. At each rate, bond rupture spectra were collected. Median forces ranged from 8 to 72 pN. These showed two linear regimes when plotted against the logarithm of the force-loading rate. However, a statistical analysis of the full rupture force spectra including the detection limits of the setup showed that all measured data are well described by dissociation over a single barrier.

SUBMITTER: Boye K 

PROVIDER: S-EPMC3882471 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Two barriers or not? Dynamic force spectroscopy on the integrin α7β1 invasin complex.

Boye Kristian K   Ligezowska Agnieszka A   Eble Johannes A JA   Hoffmann Bernd B   Klösgen Beate B   Merkel Rudolf R  

Biophysical journal 20131201 12


Dynamic force spectroscopy was used to test force-induced dissociation of the complex between the integrin α7β1 and the bacterial protein invasin. Both proteins were used in truncated forms comprising the respective binding sites. Using the biomembrane force-probe, the bond system was exposed to 14 different loading rates ranging from 18 pN/s to 5.3 nN/s. At each rate, bond rupture spectra were collected. Median forces ranged from 8 to 72 pN. These showed two linear regimes when plotted against  ...[more]

Similar Datasets

| S-EPMC6156609 | biostudies-literature
| S-EPMC1276867 | biostudies-literature
| S-EPMC4398634 | biostudies-literature
| S-EPMC1896262 | biostudies-literature
| S-EPMC5406783 | biostudies-literature
| S-EPMC11345772 | biostudies-literature
| S-EPMC10980004 | biostudies-literature
| S-EPMC3388201 | biostudies-literature
| S-EPMC6428919 | biostudies-literature
| S-EPMC8609242 | biostudies-literature