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Proteomics Using Protease Alternatives to Trypsin Benefits from Sequential Digestion with Trypsin

Therese Dau, Giulia Bartolomucci, Juri Rappsilber Analytical Chemistry, 2020 https://doi.org/10.1021/acs.analchem.0c00478 Trypsin is the most used enzyme in proteomics. Nevertheless, proteases with complementary cleavage specificity have been applied in special circumstances. In this work, we analyzed the characteristics of five protease alternatives to trypsin for protein identification and sequence coverage when applied to S. pombe whole cell lysates.

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Ultraviolet Photodissociation of Tryptic Peptide Backbones at 213 nm

Lars Kolbowski, Adam Belsom, Juri Rappsilber Journal of the American Society for Mass Spectrometry, 2020 https://doi.org/10.1021/jasms.0c00106 We analyzed the backbone fragmentation behavior of tryptic peptides of a four protein mixture and of E. coli lysate subjected to Ultraviolet Photodissociation (UVPD) at 213 nm on a commercially available UVPD-equipped tribrid mass spectrometer. We obtained 15,178 unique

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