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- W2084484966 abstract "Atomic force microscopy (AFM) is used in measuring dissociation in protein systems and protein-protein interactions forces at single molecular level. However, an explicit interpretation of the acquired rupture force data is not always easy. The Bell-Evans Standard Theory, used for analyzing rupture force data (contingent on the concept of thermal activation and the deformation of the activation barrier) yields a rupture force distribution function which is skewed to the left (towards low force). However, most of the experimental measurements of rupture force data generate a probability distribution function (pdf) with a high force tail. The probable cause of this high force tail in the rupture force pdf is either multiple attachments (though recognizable multiple ruptures are typically removed from rupture force analysis) or heterogeneous bonding. To study the effect of multiple attachments, we created a varying density of active sites using self assembled monolayer by incubating the substrate in mixed solutions of active (biotin) and inactive (methyl-terminated) PEG molecules and pursued imaging and force measurements with avidin functionalized AFM tip. Here, we present a combined approach to answer the question of how much of the high force tail can be attributed to either cause. We found that the presence of multiple attachments, while significant, accounts for only a fraction of the events in the high force tail of the distribution." @default.
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- W2084484966 date "2015-01-01" @default.
- W2084484966 modified "2023-09-29" @default.
- W2084484966 title "Effect of Surface Density of Active Sites on Rupture Force Distributions of Single Molecule Interactions" @default.
- W2084484966 doi "https://doi.org/10.1016/j.bpj.2014.11.929" @default.
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