Detecting and differentiating pivotal arginine post-translational modifications (PTMs), like methylation and citrullination, is a major challenge in proteomics. Modifications with subtle or no differences in mass are difficult to distinguish using mass spectrometry, and for all but the most highly studied proteins, ELISA PTM workflows require the generation of new antibodies and are complex, costly, and carry reproducibility challenges. These limitations constrain our understanding of proteins' roles in health and disease, particularly as arginine PTMs are known to impact cellular processes and disease states.
A novel sequencing technique overcomes these hurdles by offering enhanced sensitivity and precision in detecting arginine PTMs. This methodology, as described in the application note provided, affords a more nuanced view of protein modifications that can help shed light on intricate cellular mechanisms. Focusing on the kinetic signatures of peptide binding reveals the subtle differences in arginine PTMs, facilitating a deeper understanding of their roles and implications in biological processes.
Download this application note to discover:
- How a single-molecule sequencing solution addresses the limitations of traditional methods in detecting arginine PTMs
- Demonstrated rapid differentiation of native arginine, SDMA, and ADMA (symmetric and asymmetric dimethyl arginine respectively) as well as native arginine and citrullinated arginine residues
- The potential impact of advanced protein analysis on research and novel discoveries
