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Go beyond what you thought possible with native MS * Thermo Scientific Q Exactive UHMR Hybrid Quadrupole-Orbitrap mass spectrometer Thermo Fisher SCIENTIFIC

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Gain deeper insight into native proteins Native mass spectrometry (MS) is a powerful technique for studying the structure of large protein complexes, protein-protein, and protein-ligand interactions. The approach relies on maintaining a biomolecule’s natural folded state and associated non-covalent interactions for MS analysis. Technology limitations have prevented native MS from achieving its full potential—that is until now. The Thermo Scientific™ Q Exactive™ UHMR Hybrid Quadrupole-Orbitrap™ mass spectrometer is the first to provide the unique combination of unprecedented ultra-high mass...

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“In the analysis of large protein assemblies like viruses, ribosomes, and proteasomes, the Q Exactive UHMR mass spectrometer has made things possible that we couldn’t do before. The major benefits of the system are the substantial increase in sensitivity and resolution that we get for very large protein assemblies, together with the ability to do MS/MS experiments.” — Professor Albert Heck, Utrecht University Confidently resolve small mass differences The Q Exactive UHMR mass spectrometer resolves the small differences in masses needed to characterize large and heterogeneous intact...

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Proven Q Exactive Hybrid Quadrupole-Orbitrap technology solves native MS challenges As analytes get larger and more complex, MS system capabilities need to advance to keep pace. Built on proven Thermo Scientific™ Q Exactive™ Hybrid Quadrupole-Orbitrap™ mass spectrometer technology, the Q Exactive UHMR mass spectrometer addresses the analytical challenges inherent to native MS. A combination of Orbitrap technology enhancements come together to allow direct detection of large, intact proteins and protein complexes with unprecedented resolution and orders of magnitude more sensitivity. “For...

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Injection Flatapole HyperQuad Mass Filter with Advanced Quadrupole Technology (AQT) Advanced Active Beam Guide (AABG) 3 Orbitrap Mass Analyzer HCD Cell 1, 2 The injection flatapole is pulsed down to a negative voltage to improve desolvation of large protein complexes, while the inter-flatapole lens is maintained at a high positive potential to prevent ions from eluting out. Trapping is followed by restoration of the voltage levels, allowing low-energy elution of ions into the bent flatapole (Advanced Active Beam Guide). 3 The bent flatapole guides and focuses ions using an axial DC field...

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Remarkable sensitivity and mass resolution at high m/z enable investigation of structure and heterogeneity Use of the Q Exactive UHMR can reveal previously unknown details about biomolecular structures. Investigation of biomolecular structures such as ribosomes are challenging not only because of their size and complexity, but also because of their heterogeneity. For example, some ribosomal proteins may be present substoichiometrically, whereas other ribosomeinteracting proteins may be recruited at different stages of translation. Additionally, small modifications have been mapped to both...

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The sensitivity and resolution of Q Exactive UHMR mass spectrometer at high m/z enables analysis of intact E.coli 70S ribosome in the presence of 10 mM Mg2+ with ions centered around 36,000 m/z (left). The well-resolved charge states allow determination of the intact mass of the assembled 70S ribosome of 2,316 ± 1 kDa, which matches well with the expected mass (2,302 kDa). The mass deviation of 0.6% from the theoretical mass is mainly due to nonspecific adduction of the Mg2+ ions. With Mg2+ removal 70S particles disassemble into 30S and 50S particles (right). Distinct particles of the 30S...

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Ultra-high mass quadrupole selection and ultra-high mass range exceed previous limits The optimized Q Exactive UHMR instrument efficiently transmits and detects ions up to 80,000 m/z with unprecedented sensitivity. The spectra obtained are well resolved, allowing characterization of mixtures of protein particles, providing insights into their composition, ligand binding, and structure that are not easily obtained using other approaches. Native MS analysis of hepatitis B virus capsids under charge reducing conditions Mixtures of 3 MDa and 4 MDa hepatitis B virus capsids analyzed under charge...

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Native MS/MS analysis of hepatitis B virus capsids Relative Abundance Relative Abundance Relative Abundance Quadrupole selection The ultra-high mass selection quadrupole can be used to isolate the 4 MDa HBV particle at m/z 25,000 for subsequent fragmentation. The Q Exactive UHMR instrument confidently detects ions with m/z values up to 80,000 m/z. Here, the tandem MS spectrum of the 4 MDa HBV capsids at 300 eV HCD energy shows sequential ejection of up to 17 out of the 240 copies of the capsid protein. The ejected monomers appear at low m/z while the product ions appear at increasingly...

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Powerful native MS and native top-down analysis, in one instrument Though top-down sequencing of native protein complexes has been reported, poor fragmentation into subunits and stripped complexes in the front end of the MS have limited previous MS instruments’ ability to perform this work. The Q Exactive UHMR mass spectrometer overcomes these limitations via in-source trapping and pseudo-MS3. First, the intact protein complex is desolvated gently with moderate energy and transferred through the mass spectrometer without fragmentation, producing an MS1 spectrum. Applying more in-source...

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native MS
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