Apr 2, 2020

Mapping shifts in nanopore signal to changes in protein and protein-DNA conformation

BioRxiv : the Preprint Server for Biology
A. T. Carlsen, Vincent Tabard-Cossa


Solid-state nanopores have been used extensively in biomolecular studies involving DNA and proteins. However, the interpretation of signals generated by the translocation of proteins or protein-DNA complexes remains challenging. Here, we investigate the behavior of monovalent streptavidin and the complex it forms with short biotinylated DNA over a range of nanopore sizes, salts and voltages. We describe a simple geometric model that is broadly applicable and employ it to explain observed variations in conductance blockage and dwell time with experimental conditions. The general approach developed here underscores the value of nanopore-based protein analysis and represents progress toward the interpretation of complex translocation signals.

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Mentioned in this Paper

Acute Hemorrhage
Ebola virus
Nucleic Acid Sequencing
Public Health Service
Isolate - Microorganism

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