Premium
Advantages of high‐resolution and high‐mass range magnetic‐sector mass spectrometry for electrospray ionization
Author(s) -
Chapman John R.,
Gallagher Richard T.,
Barton E. C.,
Curtis Jonathan M.,
Derrick Peter J.
Publication year - 1992
Publication title -
organic mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 0030-493X
DOI - 10.1002/oms.1210270308
Subject(s) - mass spectrometry , fragmentation (computing) , chemistry , electrospray ionization , mass spectrum , ion , analytical chemistry (journal) , ionization , electrospray , molecule , envelope (radar) , thermal ionization mass spectrometry , resolution (logic) , spectral line , chromatography , physics , telecommunications , radar , organic chemistry , astronomy , artificial intelligence , computer science , operating system
Electrospray ionization (ESI) mass spectra have been measured on a magnetic‐sector double‐focusing mass spectrometer for a number of proteins and peptides. It is pointed out how in theory raising the mass resolution of a mass spectrometer from 800–1000 to 2400–3000 significantly increases the precision with which the envelope of isotopic peaks of a protein ion (or other organic ion) can be defined, particularly at higher masses. Better definition of the isotopic envelope ought to lead to higher precision in the experimental determination of molecular mass, which has been demonstrated. It is shown how ESI mass spectra of high‐mass molecules are significantly less congested at higher m / z values, so that for these molecules (RMM > 40 000) there is an advantage in being able to record peaks at higher m / z values ( m / z > 2000) representing ions with fewer charges. Fragmentation of a small peptide in the ESI source has been found to provide sequence information.