New Ultra-High Mass Range Mass Spectrometer Provides Solution for Analysis of Proteins and Protein Complexes
Thermo-Scientific-Q-Exactive
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Structural biologists and biopharmaceutical scientists now have access to an ultra-high mass range (UHMR) mass spectrometer (MS) that can be used to perform high quality native MS and top-down analyses and can provide novel insights into protein structure and protein-protein interactions.
The Thermo Scientific Q Exactive UHMR Hybrid Quadrupole-Orbitrap Mass Spectrometer is the first platform from Thermo Fisher Scientific to combine high resolution, high sensitivity, MS2 and pseudo-MS3 capabilities. The new system overcomes previous technology limitations that prevented native mass spectrometry from achieving its full potential and creates a workflow for the structural analysis of proteins and complexes. Thermo Fisher is showcasing the new instrument during the 66th American Society for Mass Spectrometry (ASMS) Conference, held June 3-7, in the Sapphire Ballroom ABEF at the Hilton San Diego Bayfront, San Diego.
"With the level of sensitivity and high resolution of the Q Exactive UHMR platform, researchers can better understand protein structure and interactions," said Ken Miller, vice president, omics marketing, chromatography and mass spectrometry, Thermo Fisher. "We expect the more detailed structural insights from this new system to enhance our understanding of protein function, disease mechanisms, potential drug targets and biotherapeutic compounds."
"To unlock a greater understanding of proteins and their interactions, we require substantially increased sensitivity and mass resolution at high m/z," said Albert Heck, professor, Biomolecular Mass Spectrometry and Proteomics, University of Utrecht. "This instrument enables high-fidelity, hypothesis-free mass analysis of intact ribosome particles, revealing the substoichiometric association of even elusive small proteins."
The Q Exactive UHMR mass spectrometer is designed to resolve the small differences in masses required to characterize intact biomolecular assemblies and other large molecular complexes. The new mass spectrometer can verify sample quality prior to analysis by cryo-electron microscopy (cryo-EM) and determine sample composition and homogeneity to enable successful cryo-EM analysis.
Benefits of the new system include:
• Ultra-high resolution and orders of magnitude for great sensitivity, at up to 80,000 m/z, to resolve the small differences in masses needed to characterize intact biomolecular assemblies and complexes
• In-source trapping capability that enables improved transmission and controllable desolvation and fragmentation
• High mass quadrupole selection and high HCD fragmentation efficiency for better native top-down analysis than achievable with previous Thermo Fisher technology
When analysts combine the Q Exactive UHMR mass spectrometer with the integrated Thermo Scientific BioPharma Finder 3.0 Intact software for deconvolution and Thermo Scientific ProSight software, they can elevate their research by confirming intact molecular weight of proteins and complexes as well as by obtaining sequence information and identifying potential modifications.
The Thermo Scientific Q Exactive UHMR Hybrid Quadrupole-Orbitrap Mass Spectrometer is the first platform from Thermo Fisher Scientific to combine high resolution, high sensitivity, MS2 and pseudo-MS3 capabilities. The new system overcomes previous technology limitations that prevented native mass spectrometry from achieving its full potential and creates a workflow for the structural analysis of proteins and complexes. Thermo Fisher is showcasing the new instrument during the 66th American Society for Mass Spectrometry (ASMS) Conference, held June 3-7, in the Sapphire Ballroom ABEF at the Hilton San Diego Bayfront, San Diego.
"With the level of sensitivity and high resolution of the Q Exactive UHMR platform, researchers can better understand protein structure and interactions," said Ken Miller, vice president, omics marketing, chromatography and mass spectrometry, Thermo Fisher. "We expect the more detailed structural insights from this new system to enhance our understanding of protein function, disease mechanisms, potential drug targets and biotherapeutic compounds."
"To unlock a greater understanding of proteins and their interactions, we require substantially increased sensitivity and mass resolution at high m/z," said Albert Heck, professor, Biomolecular Mass Spectrometry and Proteomics, University of Utrecht. "This instrument enables high-fidelity, hypothesis-free mass analysis of intact ribosome particles, revealing the substoichiometric association of even elusive small proteins."
The Q Exactive UHMR mass spectrometer is designed to resolve the small differences in masses required to characterize intact biomolecular assemblies and other large molecular complexes. The new mass spectrometer can verify sample quality prior to analysis by cryo-electron microscopy (cryo-EM) and determine sample composition and homogeneity to enable successful cryo-EM analysis.
Benefits of the new system include:
• Ultra-high resolution and orders of magnitude for great sensitivity, at up to 80,000 m/z, to resolve the small differences in masses needed to characterize intact biomolecular assemblies and complexes
• In-source trapping capability that enables improved transmission and controllable desolvation and fragmentation
• High mass quadrupole selection and high HCD fragmentation efficiency for better native top-down analysis than achievable with previous Thermo Fisher technology
When analysts combine the Q Exactive UHMR mass spectrometer with the integrated Thermo Scientific BioPharma Finder 3.0 Intact software for deconvolution and Thermo Scientific ProSight software, they can elevate their research by confirming intact molecular weight of proteins and complexes as well as by obtaining sequence information and identifying potential modifications.
