Protein Motion and Configurations in a Form-Fitting Nanopore: Avidin in ClyA
| Autor: | Bo Lu, Lene Vestergaard Hau, Jene Andrew Golovchenko, Chris Stokes, Monifa A. Fahie, Min Chen |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Models Molecular Movement Biophysics Biotin 02 engineering and technology 03 medical and health sciences Molecular dynamics chemistry.chemical_compound Nanopores Protein structure stomatognathic system Protein Structure Quaternary biology Chemistry Perforin Protein Conductance respiratory system 021001 nanoscience & nanotechnology Avidin Coupling (electronics) Nanopore 030104 developmental biology Biotinylation biology.protein Protein Multimerization 0210 nano-technology |
| Zdroj: | Biophysical journal. 115(5) |
| ISSN: | 1542-0086 |
| Popis: | We probe the molecular dynamics and states of an avidin 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|