From post-translational modifications to full proteome profiling and characterization

SCIEX solutions for studying protein dynamics allow researchers to reliably and reproducibly profile protein structure changes, including post-translational modifications (PTMs), using the latest innovations in fragmentation technology, which yields rich and informative MS/MS information that can unlock new biological insights. One of the greatest challenges in proteomics is the dynamic nature of proteins. PTMs such as phosphorylation, acetylation and glycosylation are common modifications that are vital to understanding biology, and they are constantly changing.

Collision-induced dissociation (CID) is one of the most common fragmentation techniques currently used in mass spectrometry. While CID produces good fragmentation across the peptide backbone for sequence determination, it can also produce side-chain fragmentation, which makes it more difficult to characterize certain PTMs.
The revolutionary ZenoTOF 7600 system features a unique electron-activated dissociation (EAD) cell that simultaneously traps precursor ions and free electrons for efficient, reproducible fragmentation. The EAD cell features tunable electron kinetic energy (KE) that can easily be adjusted to match the molecule type, giving the user precise control over MS/MS fragmentation regardless of the analyte structure, modification or charge state. And because this system has both EAD and CID fragmentation modes, it can be applied to a broader range of projects and samples and make those analyses more accessible and routine. 

PTMs add an extra challenge to the study of the proteome and the characterization of protein/peptide structures. And the extremely broad range of biological modifications that are present require powerful and flexible workflows for sample preparation through sample analysis. For mass spectrometry, this means an instrument that is both highly sensitive and flexible.

The ZenoTOF 7600 system, with EAD and CID fragmentation, allows researchers to explore a much wider range of biological questions. With higher-quality Zeno MS/MS data and robust and reproducible fragmentation, the ZenoTOF 7600 system can reliably provide a greater breadth of characterization. 

A methodology that is flexible, sensitive and reproducible is required to gain an in-depth understanding of protein structure, the specific and dynamic modifications and their biological significance on a proteome-wide scale, and to achieve confidence in results across sample sets and disease states. EAD on the ZenoTOF 7600 system gives researchers an additional fragmentation mechanism that can be used to confidently identify and quantify the structural characteristics of proteins. With the OptiFlow source, you can perform this at high throughput using microflow approach or with the highest sensitivity using a nanoflow approach.