Literature DB >> 24441471

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

Christian B Rosen1, David Rodriguez-Larrea2, Hagan Bayley3.   

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 α-hemolysin pore, enables the distinction between unphosphorylated, monophosphorylated and diphosphorylated variants. Our results provide a step toward nanopore proteomics.

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Year:  2014        PMID： 24441471      PMCID： PMC4391620          DOI： 10.1038/nbt.2799

Source DB:  PubMed          Journal:  Nat Biotechnol        ISSN： 1087-0156            Impact factor:   54.908


  47 in total

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8.  Unfoldase-mediated protein translocation through an α-hemolysin nanopore.

Authors:  Jeff Nivala; Douglas B Marks; Mark Akeson
Journal:  Nat Biotechnol       Date:  2013-02-03       Impact factor: 54.908

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Journal:  Nat Biotechnol       Date:  2008-10       Impact factor: 54.908

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  62 in total

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6.  Protein Motion and Configurations in a Form-Fitting Nanopore: Avidin in ClyA.

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7.  Electrostatic Interactions between OmpG Nanopore and Analyte Protein Surface Can Distinguish between Glycosylated Isoforms.

Authors:  Monifa A Fahie; Min Chen
Journal:  J Phys Chem B       Date:  2015-07-30       Impact factor: 2.991

8.  Channel from bacterial virus T7 DNA packaging motor for the differentiation of peptides composed of a mixture of acidic and basic amino acids.

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Journal:  Biomaterials       Date:  2019-05-21       Impact factor: 12.479

9.  Nanopores sense protein modifications.

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10.  Oriented single directional insertion of nanochannel of bacteriophage SPP1 DNA packaging motor into lipid bilayer via polar hydrophobicity.

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Journal:  Biomaterials       Date:  2016-08-04       Impact factor: 12.479
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