%0 Figure %A Fichtner, Dagmar %A Lorenz, Bärbel %A Engin, Sinem %A Deichmann, Christina %A Oelkers, Marieelen %A Janshoff, Andreas %A Menke, Andre %A Wedlich, Doris %A Franz, Clemens M. %D 2014 %T Dynamic force spectroscopy. %U https://plos.figshare.com/articles/figure/_Dynamic_force_spectroscopy_/977378 %R 10.1371/journal.pone.0093123.g006 %2 https://plos.figshare.com/ndownloader/files/1439008 %K Biochemistry %K proteins %K Protein interactions %K Recombinant proteins %K Biomacromolecule-ligand interactions %K chemical biology %K cytochemistry %K biophysics %K biotechnology %K Bioengineering %K Biological systems engineering %K Biomedical Engineering %K Biomimetics %K biomaterials %K Bionanotechnology %K cell biology %K cell adhesion %K cadherins %K Cellular structures and organelles %K Cell membranes %K Membrane proteins %K Transmembrane proteins %K Molecular cell biology %K chemistry %X

(A) Rupture force distributions obtained at different retraction speeds for the homotypic E1-5 bond rupture. (B) Rupture force Ff as a function of loading rate for homotypic E1-5 (green symbols) or heteromeric E1-2/E1-5 bond rupture (orange symbols). The different symbols represent the maxima identified in the multimodal distribution of rupture force obtained for a given loading rate. For the homotypic E1-5 bond we determined xu  =  1.1 nm and koff  =  1.2 × 10−4 s−1 (green circles); xu  =  2.3 nm and koff  =  1.4 × 10−5 s−1 (green triangles). For the heteromeric E1-5/E1-2 bond we determined xu  =  4.5 nm and koff  =  5.9 × 10−7 s−1 (yellow triangles). The violet stars indicate data taken from [41].

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