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• W2895969809 abstract "Cross-linking mass spectrometry has become an important approach for studying protein structures and protein-protein interactions. The amino acid compositions of some protein regions impede the detection of cross-linked residues, although it would yield invaluable information for protein modeling. Here, we report on a sequential-digestion strategy with trypsin and elastase to penetrate regions with a low density of trypsin-cleavage sites. We exploited intrinsic substrate-recognition properties of elastase to specifically target larger tryptic peptides. Our application of this protocol to the TAF4-12 complex allowed us to identify cross-links in previously inaccessible regions." @default.
• W2895969809 created "2018-10-26" @default.
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• W2895969809 date "2019-02-28" @default.
• W2895969809 modified "2023-10-16" @default.
• W2895969809 title "Sequential Digestion with Trypsin and Elastase in Cross-Linking Mass Spectrometry" @default.
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• W2895969809 doi "https://doi.org/10.1021/acs.analchem.8b05222" @default.
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