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Single-molecule site-specific detection of protein phosphorylation with a nanopore.

ABSTRACT: We demonstrate single-molecule, site-specific detection of protein phosphorylation with protein nanopore technology. A model protein, thioredoxin, was phosphorylated at two adjacent sites. Analysis of the ionic current amplitude and noise, as the protein unfolds and moves through an ?-hemolysin pore, enables the distinction between unphosphorylated, monophosphorylated and diphosphorylated variants. Our results provide a step toward nanopore proteomics.

SUBMITTER: Rosen CB

PROVIDER: S-EPMC4391620 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature

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Single-molecule site-specific detection of protein phosphorylation with a nanopore.

Rosen Christian B CB Rodriguez-Larrea David D Bayley Hagan H

Nature biotechnology 20140119 2

We demonstrate single-molecule, site-specific detection of protein phosphorylation with protein nanopore technology. A model protein, thioredoxin, was phosphorylated at two adjacent sites. Analysis of the ionic current amplitude and noise, as the protein unfolds and moves through an α-hemolysin pore, enables the distinction between unphosphorylated, monophosphorylated and diphosphorylated variants. Our results provide a step toward nanopore proteomics. ...[more]

PMID: 24441471

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