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Updated: Aug 19, 2026

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
Published on: October 15, 2018
Investigation of the rapid scan on an electrospray ion trap mass spectrometer
Chunguang G Yang1, Mark E Bier
1Center for Molecular Analysis, Department of Chemistry, Carnegie Mellon University, 4400 Fifth Avenue, Pittsburgh, Pennsylvania 15213, USA.
Abstract:
A rapid scan on a quadrupole ion trap mass spectrometer can improve the signal intensity by over 200 times when scanning at 12 times the normal scan rate. This intensity increase is due to a 5.5-fold increase in mass peak height due to a reduction in the mass peak width over time and a 40-fold increase in signal from the increased number of ions that can be trapped without the deleterious effects of space charge. Detection limits can be further improved by signal averaging more scans in the same period that is required for the normal scan, and the greatest advantage occurs when scanning over the full mass range. The rapid scan impacts the mass accuracy and the resolution is reduced by 6 times. The molecular weight determination of 40 fmol/microL apomyoglobin was determined in 3 s using a rapid scan, but this was not possible when using the normal scan rate. Quantitation results showed that the relative standard deviations for the total ion current peak areas of 500 fmol of angiotensin I were improved by a factor of 2.6 when the rapid scan was used.
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