ArticleProtein Motion and Configurations in a Form-Fitting Nanopore: AVIDIN (cas 1405-69-2) in ClyA

Add time:09/30/2019    Source:sciencedirect.com

We probe the molecular dynamics and states of an AVIDIN (cas 1405-69-2) protein as it is captured and trapped in a voltage-biased cytolysin A 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 cytolysin A has surprisingly rich conductance spectra that reveal transient and more permanently trapped protein configurations in the pore and how they evolve into one another. We identify a long-lasting, stable, and low-noise configuration of avidin in the nanopore into which avidin can be reliably trapped and released. This may prove useful for single-molecule studies of other proteins that can be biotinylated and then transported by avidin to the pore via their coupling to avidin with biotin-avidin linking. We demonstrate the sensitivity of this system with detection of biotin attached to avidin captured by the pore.

We also recommend Trading Suppliers and Manufacturers of AVIDIN (cas 1405-69-2). Pls Click Website Link as below: cas 1405-69-2 suppliers

Prev:Interactions between AVIDIN (cas 1405-69-2) and graphene for development of a biosensing platform
Next:Comparative FTIR spectroscopic study upon the hydration of lecithins and CEPHALIN (cas 1405-71-6)s)