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- W4309148772 abstract "ABSTRACT Significant recent advances in structural biology, particularly in the field of cryo-electron microscopy, have dramatically expanded our ability to create structural models of proteins and protein complexes. However, many proteins remain refractory to these approaches because of their low abundance, low stability or – in the case of complexes – simply not having yet been analysed. Here, we demonstrate the power of combining cross-linking mass spectrometry (XL-MS) with artificial intelligence-based structure prediction to discover and experimentally substantiate models for protein and protein complex structures at proteome scale. We present the deepest XL-MS dataset to date, describing 28,910 unique residue pairs captured across 4,084 unique human proteins and 2,110 unique protein-protein interactions. We show that integrative models of complexes driven by AlphaFold Multimer and inspired and corroborated by the XL-MS data offer new opportunities to deeply mine the structural proteome and interactome and reveal new mechanisms underlying protein structure and function." @default.
- W4309148772 created "2022-11-23" @default.
- W4309148772 creator A5010727704 @default.
- W4309148772 creator A5020208790 @default.
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- W4309148772 creator A5085394688 @default.
- W4309148772 creator A5088886897 @default.
- W4309148772 date "2022-11-16" @default.
- W4309148772 modified "2023-09-27" @default.
- W4309148772 title "Cross-linking mass spectrometry discovers, evaluates, and validates the experimental and predicted structural proteome" @default.
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