Fourier transform mass spectrometry is the key performance characteristics of fourier transform-based mass spectrometry, mass accuracy and resolution are presented in the view of how they impact the interpretation of measurements in proteomic applications. The motion of ions in a Fourier Transform Mass Spectrometry analyzer can understand by the magnetic and electric fields present in the FTMS analyzer cell. The FTMS experiment is a series of events like ionization, excitation and detection that occur in sequence. Fourier transformation of the time domain signal results in the frequency domain FT-ICR signal which, on the basis of the inverse proportionality between frequency and m/z ratio, can be converted to a mass spectrum. The ions are to be detected, with a selected m/z ratio, absorb maximum energy through the effect of a high-frequency field and a constant magnetic field perpendicular to it. Maximum energy is gained by ions that satisfy the cyclotron resonance condition and as a result these are separated from ions of different mass/charge. The advantages of fourier transform mass spectrometry includes High mass resolution, accuracy of mass determination and structure-specific fragmentation.
Related journals of Fourier Transform Mass Spectrometry
Journal of Proteomics & Bioinformatics, Journal of Pharmacogenomics & Pharmacoproteomics, Journal of Chromatography & Separation Techniques, Industrial Chemistry: Open Access, Journal of Chromatographic Science, Chromatography Research International and Journal of Liquid Chromatography & Related Technologies
