bioRxiv preprint doi: https://doi.org/10.1101/2021.04.13.439572; this version posted April 13, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC 4.0 International license. Proteome-scale amino-acid resolution footprinting of protein-binding sites in the intrinsically disordered regions of the human proteome Caroline Benz1,*, Muhammad Ali1,*, Izabella Krystkowiak2,* , Leandro Simonetti1, Ahmed Sayadi1, Filip Mihalic3, Johanna Kliche1, Eva Andersson3, Per Jemth3, Norman E. Davey2,#, Ylva Ivarsson1, # Affiliations: 1. Department of Chemistry - BMC, Uppsala University, Box 576, Husargatan 3, 751 23 Uppsala, Sweden 2. Division of Cancer Biology, The Institute of Cancer Research, 237 Fulham Road, London SW3 6JB, UK. 3. Department of Medical Biochemistry and Microbiology, Uppsala University, Box 582, Husargatan 3, 751 23 Uppsala Sweden * Equal contribution # Corresponding authors:
[email protected] [email protected] 1 bioRxiv preprint doi: https://doi.org/10.1101/2021.04.13.439572; this version posted April 13, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC 4.0 International license. Abstract Specific protein-protein interactions are central to all processes that underlie cell physiology. Numerous studies using a wide range of experimental approaches have identified tens of thousands of human protein-protein interactions. However, many interactions remain to be discovered, and low affinity, conditional and cell type-specific interactions are likely to be disproportionately under-represented.