Cross-linking mass spectrometry for mapping protein complex topologies in situ

Cross-linking mass spectrometry has become an established technology to provide structural information on the topology and dynamics of protein complexes. Readily accessible workflows can provide detailed data on simplified systems, such as purified complexes. However, using this technology to study...

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Vydáno v:Essays in biochemistry Ročník 67; číslo 2; s. 215
Hlavní autoři: Lee, Kitaik, O'Reilly, Francis J
Médium: Journal Article
Jazyk:angličtina
Vydáno: England 29.03.2023
Témata:
Cross-Linking Reagents - chemistry
Cross-Linking Reagents - metabolism
Mass Spectrometry - methods
Proteomics - methods
Crosslinking
proteomics
in situ
protein-protein interactions
ISSN:1744-1358, 1744-1358
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Shrnutí:Cross-linking mass spectrometry has become an established technology to provide structural information on the topology and dynamics of protein complexes. Readily accessible workflows can provide detailed data on simplified systems, such as purified complexes. However, using this technology to study the structure of protein complexes in situ, such as in organelles, cells, and even tissues, is still a technological frontier. The complexity of these systems remains a considerable challenge, but there have been dramatic improvements in sample handling, data acquisition, and data processing. Here, we summarise these developments and describe the paths towards comprehensive and comparative structural interactomes by cross-linking mass spectrometry.
Bibliografie:ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
ISSN:1744-1358
1744-1358
DOI:10.1042/EBC20220168