A calibration routine for efficient ETD in large-scale proteomics

J Am Soc Mass Spectrom. 2015 Nov;26(11):1848-57. doi: 10.1007/s13361-015-1183-1. Epub 2015 Jun 26.

Abstract

Electron transfer dissociation (ETD) has been broadly adopted and is now available on a variety of commercial mass spectrometers. Unlike collisional activation techniques, optimal performance of ETD requires considerable user knowledge and input. ETD reaction duration is one key parameter that can greatly influence spectral quality and overall experiment outcome. We describe a calibration routine that determines the correct number of reagent anions necessary to reach a defined ETD reaction rate. Implementation of this automated calibration routine on two hybrid Orbitrap platforms illustrate considerable advantages, namely, increased product ion yield with concomitant reduction in scan rates netting up to 75% more unique peptide identifications in a shotgun experiment. Graphical Abstract ᅟ.

Keywords: Calibration; ETD; Ion/ion; Kinetics; Mass spectrometry; Orbitrap; Proteomics.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Calibration
  • Kinetics
  • Peptides / analysis
  • Peptides / chemistry
  • Proteomics / methods*
  • Proteomics / standards*
  • Tandem Mass Spectrometry / methods*
  • Tandem Mass Spectrometry / standards*

Substances

  • Peptides