Protein Motion and Configurations in a Form-Fitting Nanopore: Avidin in ClyA

We probe the molecular dynamics and states of an avidin protein as it is captured and trapped in a voltage biased ClyA nanopore using time-resolved single-molecule electrical conductance signals. The data for very large numbers of single-molecule events are analyzed and presented by a new method that provides clear visual insight into the molecular scale processes. Avidin in ClyA has surprisingly rich conductance spectra that reveal transient and more permanently trapped protein configurations in the pore and how they evolve into one another.

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