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Publication - Professor Imre Berger

    Sequential Digestion with Trypsin and Elastase in Cross-Linking Mass Spectrometry


    Dau, T, Gupta, K, Berger, I & Rappsilber, J, 2019, ‘Sequential Digestion with Trypsin and Elastase in Cross-Linking Mass Spectrometry’. Analytical Chemistry, vol 91., pp. 4472-4478


    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.

    Full details in the University publications repository