Abstract:
:A theoretical framework is developed to analyze molecular bond breaking in dynamic force spectroscopy using atomic force microscopy (AFM). An analytic expression of the observed bond breaking probability as a function of force is obtained in terms of the relevant physical parameters. Three different experimental realizations are discussed, in which (i) the force is increased linearly in time, and (ii) the AFM cantilever is moved at constant speed, and (iii) the force is held constant. We find that unique fitting of the bond parameters such as the potential depth and its width is possible only when data from rather different force-loading rates is used. The complications in the analysis of using the constant velocity mode arising from the intermediate polymer spacer are discussed at length.
journal_name
Biointerphasesjournal_title
Biointerphasesauthors
Hanke F,Kreuzer HJdoi
10.1116/1.2188519subject
Has Abstractpub_date
2006-03-01 00:00:00pages
11issue
1eissn
1934-8630issn
1559-4106journal_volume
1pub_type
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