Two-dimensional mass spectrometry of biomolecules at the subfemtomole level

Fred W. McLafferty*, Neil L. Kelleher, Tadhg P. Begley, Einar K. Fridriksson, Roman A. Zubarev, David M. Horn

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

38 Scopus citations

Abstract

Multiple dimensions of unique molecular structure information can now be obtained from proteins and DNA using mass spectrometry. Less than 10-6 mol of the active major histocompatibility complex signaling peptide in a mixture of thousands can be identified. For large proteins (>40 kDa), the high resolving power (>105) and 10-17 mol sensitivity of Fourier-transform mass spectrometry provide exact molecular weight values (± 1 or 2 Da) for mixture components, indicating errors or modifications compared with the predicted DNA sequence. Selecting a specific molecular species, its two-dimensional spectrum indicates the part of the molecule that is modified; a three-dimensional spectrum of that fragment further isolates the modification site.

Original languageEnglish (US)
Pages (from-to)571-578
Number of pages8
JournalCurrent Opinion in Chemical Biology
Volume2
Issue number5
DOIs
StatePublished - Jan 1 1998

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry

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