期刊
STRUCTURE
卷 30, 期 4, 页码 441-461出版社
CELL PRESS
DOI: 10.1016/j.str.2022.03.003
关键词
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资金
- ETH Zurich [ETH-24 16-2]
- ETH Domain Strategic Focus Area Personalized Health and Related Technologies [PHRT-503]
- Swiss National Science Foundation through the National Center of Competence in Research, RNA & Disease (NCCR RNA Disease)
- National Research Programme Covid-19 [NRP 78]
- SNSF individual project [200679]
Cross-linking and mass spectrometry (XL-MS) workflows are increasingly popular for low-resolution structural studies of macromolecular complexes. Protein-protein XL-MS protocols are widely adopted, while protein-RNA XL-MS workflows are evolving rapidly.
Cross-linking and mass spectrometry (XL-MS) workflows represent an increasingly popular technique for low-resolution structural studies of macromolecular complexes. Cross-linking reactions take place in the solution state, capturing contact sites between components of a complex that represent the native, functionally relevant structure. Protein-protein XL-MS protocols are widely adopted, providing precise localization of cross-linking sites to single amino acid positions within a pair of cross-linked peptides. In contrast, protein-RNA XL-MS workflows are evolving rapidly and differ in their ability to localize interaction regions within the RNA sequence. Here, we review protein-protein and protein-RNA XL-MS workflows, and discuss their applications in studies of protein-RNA complexes. The examples highlight the complementary value of XL-MS in structural studies of protein-RNA complexes, where more established high-resolution techniques might be unable to produce conclusive data.
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