Single-molecule identification of full-length proteins with single-amino-acid resolution using nanopores
Discovered via OpenAlex
Preprint source: bioRxiv: Biophysics
Curated by Nanopore Foundations & Signal Analysis · Electroosmotic flow · Identification · Preprint · Protein analysis · Unfoldase-driven transport
Abstract
Nanopore-based technologies show promise in single-molecule protein sequencing. By using an unfoldase and a nanopore with enhanced electroosmotic flow, here we show the continuous identification of generic proteins during single nanopore passes. This approach enables the recording of differences in charge and size from single amino acid substitutions compared to reference signals, paving the way for single-molecule protein sequencing and high-throughput proteomics.