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Kang, H. FT-ICR Mass Spectrometry. Encyclopedia. Available online: https://encyclopedia.pub/entry/60687 (accessed on 12 November 2026).
Kang H. FT-ICR Mass Spectrometry. Encyclopedia. Available at: https://encyclopedia.pub/entry/60687. Accessed November 12, 2026.
Kang, Helena. "FT-ICR Mass Spectrometry" Encyclopedia, https://encyclopedia.pub/entry/60687 (accessed November 12, 2026).
Kang, H. (2026, October 08). FT-ICR Mass Spectrometry. In Encyclopedia. https://encyclopedia.pub/entry/60687
Kang, Helena. "FT-ICR Mass Spectrometry." Encyclopedia. Web. 08 October, 2026.

FT-ICR Mass Spectrometry

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Ion cyclotron motion in a strong magnetic field, recorded as an image-current transient and converted by Fourier transformation into a frequency-domain mass spectrum, defines Fourier-transform ion-cyclotron-resonance (FT-ICR) mass spectrometry. Trapped ions orbit at a cyclotron frequency inversely proportional to their mass-to-charge ratio; broadband excitation and detection of that motion yield ultra-high mass resolving power and mass accuracy [1]. The same trapped-ion population can be activated by collisions or by electron capture, so that tandem spectra report connectivity without leaving the ICR cell [2]. Conceptual boundaries exclude quadrupole, time-of-flight, and Orbitrap Fourier-transform instruments that do not use cyclotron motion in a homogeneous magnet, although all Fourier-transform mass spectrometers share the time-to-frequency conversion step. Essential features are a high-field magnet, an ion trap that supports coherent cyclotron motion, and a Fourier-transform data system. Exact-composition assignment in complex mixtures and localization of noncovalent ligand sites are analytical consequences of the mass accuracy and tandem capabilities inherent in the ICR measurement principle [3]. An FT-ICR spectrum of dissolved organic matter is correspondingly interpreted as a catalogue of exact molecular compositions rather than as a chromatographic retention map [4].

FT-ICR ion cyclotron resonance Fourier transform high-resolution mass spectrometry
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References

  1. Stephen C. Brown; Gary Kruppa; Jean‐Louis Dasseux; Metabolomics applications of FT‐ICR mass spectrometry. Mass Spectrom. Rev. 2004, 24, 223-231. [CrossRef]
  2. Julia Laskin; Jean H. Futrell; Collisional activation of peptide ions in FT‐ICR mass spectrometry. Mass Spectrom. Rev. 2003, 22, 158-181. [CrossRef]
  3. Yongming Xie; Jennifer Zhang; Sheng Yin; Joseph A. Loo; Top-Down ESI-ECD-FT-ICR Mass Spectrometry Localizes Noncovalent Protein-Ligand Binding Sites. J. Am. Chem. Soc. 2006, 128, 14432-14433. [CrossRef]
  4. Chen He; Yahe Zhang; Yunyun Li; Xiaocun Zhuo; Yuguo Li; Chuanlun Zhang; Quan Shi; In-House Standard Method for Molecular Characterization of Dissolved Organic Matter by FT-ICR Mass Spectrometry. ACS Omega 2020, 5, 11730-11736. [CrossRef]
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Entry Collection: Analytical Chemistry
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Update Date: 21 Oct 2026
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