Achieving insights into the structure of proteins and protein macromolecular complexes is critical in understanding the relationship with their biological function.
Using either HDX-MS or Native MS analysis, the SELECT SERIES Cyclic IMS can help your lab learn about the physical size and shape of proteins, and is ideal for modeling protein assembly structures that are difficult and time-consuming to study with conventional structural biology approaches.
For studying protein unfolding and subunit configurations, the Cyclic IMS can be configured with an array of ion activation techniques, including electron capture dissociation (ECD), surface induced dissociation (SID), and collision-induced dissociation (CID). All of these techniques combine with scalable ion mobility and IMSn to deliver unique insights in structure.
Interrogate heterogeneous protein assemblies in the 10 kDa to 1 MDa range with the SELECT SERIES Cyclic IMS ion mobility mass spectrometry, ideal for intact in the gas phase and for structural biology analysis.
Improve your post-translational modification studies with the SYNAPT XS that uniquely implements electron-transfer dissociation (ETD) in the trap-region of the TriWave device for the optional, supplemental activation of ions by collision-induced dissociation (CID).
Get the robust solution you need for protein drug discovery and development and higher order structure studies with Waters HDX MS LC-MS, automation, and informatics solutions.
Accelerate your research and comprehensively identify analytes in complex samples with the SELECT SERIES MRT that provides a unique combination of ultra-high resolution and specificity independent of scan speed, for unambiguous compound identification with even the most complex samples.
Extracted ion mobilogram at 597.34 m/z corresponding to the peptide GIIQPQQPAQL with one deamidated glutamine residue (out of a possible four). Based on drift time after five passes, four different species could be separated.
Resolving deamidations for confident quantification. A) The deamidated forms of peptide HC:T23 elute in the tail of the native peptide peak.
Without the ultra-high resolution of the SELECT SERIES MRT as shown in (B) identification and quantification of the deamidations.
Representative MaxEnt1 deconvolution of trastuzumab from denaturing analysis (10 ng injection).
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