FT-ICR MS (Fourier Transform Ion Cyclotron Resonance Mass Spectrometry)

Key Features Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

• In FT-ICR MS, the detection process is non-destructive, enabling experiments such as multi-stage mass spectrometry (MSⁿ), ion–molecule interactions, and isotope exchange studies. Furthermore, an infrared laser can be directed into the ICR cell to intersect the trapped ion packet, allowing the acquisition of infrared spectra via photofragmentation.
• The mass spectrometer features a comprehensive database of expert odor profiles, ultra-sensitive analysis with multiple column options, threshold detection through multiple reaction monitoring (MRM) and selected ion monitoring (SIM) modes, and a predicted retention time display function.
• The system offers a dynamic range exceeding five orders, mass accuracy better than 2 ppm, and resolution greater than 60,000 (R). It delivers high sensitivity with a signal-to-noise ratio of at least 200:1 for 20 fg of 2,3,7,8-tetrachlorodibenzo-p-dioxin. In addition, it is equipped with turbo molecular pumps and advanced software for automated tuning and quantitative analysis.
• This instrument enables simultaneous measurement of all five argon isotopes, offering high sensitivity, advanced detection technologies, and exceptional precision for noble gas isotope ratio analysis. Its compact design, innovative emission suppression and amplifier technologies, and fully integrated software provide unmatched stability, flexibility, and control for a wide range of applications.

Applications FT-ICR High-Resolution Mass Spectrometry

• High-resolution characterization of protein assemblies: FT-ICR mass spectrometry enables precise determination of protein oligomerization states by resolving isotopic distributions, thereby distinguishing between monomers, dimers, and higher-order assemblies. Its ultrahigh resolution also allows detection of subtle mass shifts, such as those caused by disulfide bond formation, providing critical insights into protein structure and interactions.
• Metal ion binding: The technique enables precise characterization of protein–metal ion interactions, even in complex mixtures with subtle mass differences. It allows differentiation of overlapping isotope distributions, revealing cooperative binding events and metal-induced structural variations in proteins.
• Conformational analysis: FT-ICR-MS, combined with hydrogen/deuterium (H/D) exchange, enables the detection and resolution of multiple protein conformations by distinguishing overlapping isotope distributions with ultrahigh accuracy. It also provides insights into structural dynamics, such as folding states and ligand-induced conformational changes, at both solution and gas phases.
• Electron capture dissociation: The method, combined with electron capture dissociation (ECD), enables extensive peptide and protein sequencing by producing high sequence coverage and preserving post-translational modifications. It further helps in the identification of specific bond cleavages, including disulfide bonds, which are difficult to resolve with other dissociation techniques.
• Sustained off-resonance irradiation collision-induced dissociation (SORI-CID) of protein complexes: FT-ICR-MS combined with SORI-CID enables the controlled dissociation of protein complexes in the gas phase, providing insights into quaternary structure and subunit interactions. This approach preserves information about solution-phase memory, allowing the identification of specific binding sites, salt bridges, and stability differences among protein–ligand assemblies.
• Characterization of natural organic matter: The mass spectrometry method provides molecular characterization of natural organic matter (NOM), enabling precise formula assignment and component classification despite its inherent complexity. Coupled with complementary analytical methods, FT-ICR MS enhances confidence in compositional analysis and offers deep insights into NOM structure and properties.
• Clinical, food, and environmental research: FT-ICR MS enables the high-confidence identification of metabolites and proteins associated with diseases such as Alzheimer’s and type 2 diabetes. Beyond human health, it has been applied to plant and animal metabolomics, aiding in the characterization of complex metabolomes and the development of new reference databases. Additionally, FT-ICR MS is increasingly used in food, beverage, and environmental studies, where its high resolution and isotopic fine structure analysis support authentication, contaminant detection, and monitoring of ecological processes.

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