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- W3041387264 abstract "Abstract Cross-linking mass spectrometry has developed into an important method to study protein structures and interactions. The in-solution cross-linking workflows involve time and sample consuming steps and do not provide sensible solutions for differentiating cross-links obtained from co-occurring protein oligomers, complexes, or conformers. Here we developed a cross-linking workflow combining blue native PAGE with in-gel cross-linking mass spectrometry (IGX-MS). This workflow circumvents steps, such as buffer exchange and cross-linker concentration optimization. Additionally, IGX-MS enables the parallel analysis of co-occurring protein complexes using only small amounts of sample. Another benefit of IGX-MS observed by experiments on GroEL and purified bovine heart mitochondria, is the substantial reduction of artificial over-length cross-links when compared to in-solution cross-linking. We next used IGX-MS to investigate the complement components C5, C6, and their hetero-dimeric C5b6 complex. The obtained cross-links were used to generate a refined structural model of the complement component C6, resembling C6 in its inactivated state. This finding shows that IGX-MS can be used to provide new insights into the initial stages of the terminal complement pathway." @default.
- W3041387264 created "2020-07-16" @default.
- W3041387264 creator A5001113054 @default.
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- W3041387264 date "2020-07-10" @default.
- W3041387264 modified "2023-10-06" @default.
- W3041387264 title "Selective cross-linking of coinciding protein assemblies by in-gel cross-linking mass-spectrometry" @default.
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- W3041387264 doi "https://doi.org/10.1101/2020.07.10.193003" @default.
- W3041387264 hasPublicationYear "2020" @default.
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