Single-molecule site-specific detection of protein phosphorylation with a nanopore.
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.
1] Department of Chemistry, University of Oxford, Oxford, UK. [2] Center for DNA Nanotechnology, Department of Chemistry and iNANO, Aarhus University, Aarhus, Denmark. [3].
Christian B
CB
Rosen
1] Department of Chemistry, University of Oxford, Oxford, UK. [2].
David
D
Rodriguez-Larrea
Department of Chemistry, University of Oxford, Oxford, UK.
Hagan
H
Bayley
D000595:Amino Acid Sequence; D001709:Biotechnology / Q000379:methods*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D058608:Nanopores; D010766:Phosphorylation; D011506:Proteins / Q000032:analysis* / Q000737:chemistry* / Q000378:metabolism; D040901:Proteomics; D016415:Sequence Alignment
D011506:Proteins