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Best practices and benchmarks for intact protein analysis for top-down mass spectrometry
- Donnelly, Daniel P;
- Rawlins, Catherine M;
- DeHart, Caroline J;
- Fornelli, Luca;
- Schachner, Luis F;
- Lin, Ziqing;
- Lippens, Jennifer L;
- Aluri, Krishna C;
- Sarin, Richa;
- Chen, Bifan;
- Lantz, Carter;
- Jung, Wonhyeuk;
- Johnson, Kendall R;
- Koller, Antonius;
- Wolff, Jeremy J;
- Campuzano, Iain DG;
- Auclair, Jared R;
- Ivanov, Alexander R;
- Whitelegge, Julian P;
- Paša-Tolić, Ljiljana;
- Chamot-Rooke, Julia;
- Danis, Paul O;
- Smith, Lloyd M;
- Tsybin, Yury O;
- Loo, Joseph A;
- Ge, Ying;
- Kelleher, Neil L;
- Agar, Jeffrey N
- et al.
Published Web Location
https://doi.org/10.1038/s41592-019-0457-0Abstract
One gene can give rise to many functionally distinct proteoforms, each of which has a characteristic molecular mass. Top-down mass spectrometry enables the analysis of intact proteins and proteoforms. Here members of the Consortium for Top-Down Proteomics provide a decision tree that guides researchers to robust protocols for mass analysis of intact proteins (antibodies, membrane proteins and others) from mixtures of varying complexity. We also present cross-platform analytical benchmarks using a protein standard sample, to allow users to gauge their proficiency.
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