@article {365,
	title = {Multiple rereads of single proteins at single{\textendash}amino acid resolution using nanopores},
	journal = {Science},
	volume = {374},
	year = {2021},
	month = {11/2021},
	pages = {1509{\textendash}1513},
	abstract = {<p>A proteomics tool capable of identifying single proteins would be important for cell biology research and applications. Here, we demonstrate a nanopore-based single-molecule peptide reader sensitive to single{\textendash}amino acid substitutions within individual peptides. A DNA-peptide conjugate was pulled through the biological nanopore MspA by the DNA helicase Hel308. Reading the ion current signal through the nanopore enabled discrimination of single{\textendash}amino acid substitutions in single reads. Molecular dynamics simulations showed these signals to result from size exclusion and pore binding. We also demonstrate the capability to {\textquotedblleft}rewind{\textquotedblright} peptide reads, obtaining numerous independent reads of the same molecule, yielding an error rate of \&lt;10<sup>-6</sup>\&nbsp;in single amino acid variant identification. These proof-of-concept experiments constitute a promising basis for the development of a single-molecule protein fingerprinting and analysis technology.</p>
},
	doi = {10.1021/acs.nanolett.1c04203},
	author = {Brinkerhoff, Henry and Kang, Albert SW and Liu, Jingqian and Aleksei Aksimentiev and Dekker, Cees}
}
