Fourier-transform ion cyclotron resonance mass spectrometry is a type of mass analyzer (or mass spectrometer) for determining the mass-to-charge ratio (m / z) of ions based on the cyclotron frequency of the ions in a fixed magnetic field. [1] The ions are trapped in a Penning trap (a magnetic field with electric trapping plates), where they are …

Mar 12, 2004 · Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry has become increasingly significant within recent years. The inherently ultra-high resolution and mass accuracy allow unequivocal assignments of chemical formulae to be made and further structural elucidation can be conducted through the utilization of tandem mass spectrometry ...

For many years, the Fourier Transform Ion Cycloctron Resonance (FT-ICR) mass analyzer has been one of the most powerful options in terms of mass resolution and mass accuracy. Mass analysis is performed by measuring the frequencies of ion motion inside a magnetic field via "image current" detection.

Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR-MS) is a trapped ion technique that determines the cyclotron frequency of ions trapped in a Penning trap inserted in a strong magnetic field.

For this we use a Fourier transform ion cyclotron resonance mass spectrometer (FT-ICR MS). In this technique, the mass-to-charge ratio (m/z) of an ion can be experimentally determined by measuring the frequency at which the ion processes in a magnetic field.

Fourier-transform ion cyclotron resonance (FT-ICR) mass spectrometry (MS) remains the technique of choice for the analysis of intact proteins from complex biological systems, i.e. top-down proteomics.

Feb 1, 2015 · This article reviews the development of Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) in several respects: (a) a strong static magnetic field serves to convert ion mass-to-charge ratio into cyclotron frequency.

Feb 10, 2014 · Fourier transform ion cyclotron resonance (FT ICR) mass spectrometer offers highest resolving power and mass accuracy among all types of mass spectrometers. Its unique analytical characteristics made FT ICR important tool for proteomics, metabolomics, petroleomics, and investigation of complex mixtures.

A major contributor to these advances is FT-ICR-MS technology and its implementation with accurate mass measurements on cross-linked peptide pair precursor and fragment ions to enable improved identification methods.

We are able to explain the fundamental FT-ICR phenomena from a simplified theoretical treatment of ion behavior in idealized magnetic and electric fields.