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Mass Spectrometry Instrumentation
Published in Grinberg Nelu, Rodriguez Sonia, Ewing’s Analytical Instrumentation Handbook, Fourth Edition, 2019
Yuan Su, Li-Rong Yu, Thomas P. Conrads, Timothy D. Veenstra
The performance capabilities of FTICR make it a potentially powerful tool in the characterization of global proteome mixtures. One of its most significant advantages compared with other types of mass analyzer is its wide dynamic range. This wide dynamic range enables the identification of low-abundance species in the presence of higher-abundance components. The high mass accuracy of FTICR (potentially <1 ppm) also enables it to conduct multiplexed MS/MS studies in which multiple ions are accumulated and fragmented in a single scan and the product ions correctly assigned to their parent ion (Li et al., 2001). This multiplexed capability has the potential to significantly increase the number of species that can be identified within a single LC/MS/MS analysis compared with the existing conventional technologies. FTICR has been equipped with both MALDI and ESI sources, enabling it to be coupled with online LC and electrophoretic separations. Although it is still a very expensive and somewhat technically challenging technology, these scenarios are rapidly changing with some of the new Fourier transform mass spectrometry (FT-MS) instruments becoming commercially available. FTICR-MS provides proteomic analysis with an ultra-high-resolution platform for analyzing drug–antibody conjugate (Rosati et al., 2013), proteins (Weisbrod et al., 2017), and peptides (Nicolardi et al., 2015) with a combination of various dissociation methods. FTICR-MS also improves the accuracy of mass spectrometry imaging so as to link images of proteins with the proteomics data (Spraggins et al., 2015). This technique has already been used for analyzing metabolites from formalin-fixed, paraffin-embedded clinical tissue samples (Buck et al., 2015).
Characterization of harmonics and multi-charged peaks obtained by Fourier transform ion cyclotron resonance mass spectrometry
Published in Instrumentation Science & Technology, 2018
Fourier transform ion cyclotron resonance mass spectrometry (FTICR MS) is characterized by high resolution, high-quality detection limit, high scanning speed, wide dynamic range, high quality accuracy, and other technical advantages and is therefore widely used in forensic identification, metabonomics, natural products, and food science.[1234567891011121314151617] FTICR MS is based on the principle that charged particles gyrate with a cyclotron frequency that is proportional to their charge and mass, that is, m/q:ωc = qB/m. Although the ion motion equation is linear, the ion cyclotron resonance (ICR) cell has a nonlinear response, which produces a transient signal, including frequency, mass spectrum, and some additional peaks. The peaks that correspond to the harmonics of the fundamental frequencies may appear in the spectrum.[18] Specifically, if a signal is periodic with frequency f, then the only frequencies comprising the signal are integer multiples of f: f, 2f, 3f, 4f, and so on. These frequencies are called harmonics.[19]
Molecular-level exploration of properties of dissolved organic matter in natural and engineered water systems: A critical review of FTICR-MS application
Published in Critical Reviews in Environmental Science and Technology, 2023
Mingqi Ruan, Fengchang Wu, Fuhong Sun, Fanhao Song, Tingting Li, Chen He, Juan Jiang
FTICR-MS has several powerful advantages and unique functions to decipher the “black box” of aquatic DOM, benefiting researchers to overcome technical challenges in DOM research. First, FTICR-MS has high resolution and mass accuracy, which achieves peak separation within an extremely small mass unit, overcoming the technical challenges of insufficient molecular information obtained by traditional low-resolution spectrometry. The low-resolution mass spectrum does not allow peak separation to distinguish molecules whose mass changes are less than one mass unit (Sleighter & Hatcher, 2007). However, the mass resolving power of FTICR-MS can reach more than 30000, and the errors in m/z value for single DOM molecule can be less than 0.5 ppm (Qi et al., 2022). Mass differences of a few millidaltons can be distinguished by FTICR-MS, which improves the ability to assign unique DOM molecules (Hsu et al., 2011). Second, electrospray ionization (ESI) of FTICR-MS preserves molecular integrity as much as possible by simplifying injection process, which allows the infusion of aqueous solutions into the mass spectrometer and coupling of mass spectrometry with liquid chromatography (Reemtsma, 2009). This overcomes the technical challenges of destructing and derivatizing DOM molecules and allows the direct analysis of complex DOM. Third, FTICR-MS presents composition and chemical reactions at the molecular level of DOM mixtures. This overcomes the technical challenges of identifying the molecular diversity in composition and transformation of aquatic DOM during various environmental processes. The abundant molecular formulas make FTICR-MS currently one of the few techniques available to observe majority individual DOM components (Minor et al., 2014). Compared to spectroscopy, specific FTICR-MS molecular formulas and indicators help explore deeper understanding of DOM properties. However, several drawbacks and limitations of FTICR-MS also need to be considered (see details in the section 6.1).