Methods and error estimations of uncertainties in single-molecule dynamic force spectroscopy
2009 (English)In: European Biophysics Journal, ISSN 0175-7571, E-ISSN 1432-1017, Vol. 38, no 7, 911-922 p.Article in journal (Refereed) Published
In dynamic force spectroscopy, access to the characteristic parameters of single molecular bonds requires non-trivial measurements and data processing as the rupture forces are found not only to be distributed over a wide range, but are also dependent on the loading rate. The choice of measurement procedure and data processing methods has a considerable impact on the accuracy and precision of the final results. We analyse, by means of numerical simulations, methods to minimize and assess the magnitude of the expected errors for different combinations of experimental and evaluation methods. It was found that the choice of fitting function is crucial to extract correct parameter values. Applying a Gaussian function, which is a common practice, is equivalent to introducing a systematic error, and leads to a consequent overestimation of the thermal off-rate by more than 30%. We found that the precision of the bond length and the thermal off-rate, in presence of unbiased noise, were improved by reducing the number of loading rates for a given number of measurements. Finally, the results suggest that the minimum number of measurements needed to obtain the bond strength, with acceptable precision, exceeds the common number of ~100 reported in literature.
Place, publisher, year, edition, pages
2009. Vol. 38, no 7, 911-922 p.
Specific Binding, DFS, Receptor-ligand, Error Propagation, Bond Length, Thermal off-rate, Monte Carlo Simulation
Other Physics Topics
Research subject Physics
IdentifiersURN: urn:nbn:se:umu:diva-21485DOI: 10.1007/s00249-009-0471-8ISI: 000269055500009OAI: oai:DiVA.org:umu-21485DiVA: diva2:211324