@techreport{34455c4260164854b659661c568ce868,
title = "Full-Length Single-Molecule Protein Fingerprinting",
abstract = "Proteins are the primary functional actors of the cell. Hence, their identification is pivotal to advance our understanding of cell biology and disease. Current protein analysis methods are of limited use for distinguishing proteoforms. In particular, mass spectrometric methods often provide only ambiguous information on post-translational modification sites, and sequences of co-existing modifications may not be resolved. Here we demonstrate FRET-based single-molecule protein fingerprinting to map the location of individual amino acids and a post-translational modification within single full-length protein molecules. Using an approach that relies on transient binding of fluorescently labeled DNA strands to probe the amino acids on a protein one by one we show that we can fingerprint intrinsically disordered proteins as well as folded globular proteins with sub-nanometer resolution. We anticipate that this technology will be used for proteoform identification in biological and translational research with ultimate sensitivity.",
author = "Mike Filius and Wee, {Raman van} and Lannoy, {Carlos de} and Ilja Westerlaken and Zeshi Li and Kim, {Sung Hyun} and Pinto, {Cecilia de Agrela} and Yunfei Wu and Geert-Jan Boons and Martin Pabst and Ridder, {Dick de} and Chirlmin Joo",
year = "2023",
month = sep,
day = "28",
doi = "10.1101/2023.09.26.559471",
language = "English",
series = "bioRxiv",
publisher = "bioRxiv",
type = "WorkingPaper",
institution = "bioRxiv",
}