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

doi:10.1016/S1367-5931(98)80085-9

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

Molecular Biosciences

Research output: Contribution to journal › Article › peer-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 language	English (US)
Pages (from-to)	571-578
Number of pages	8
Journal	Current Opinion in Chemical Biology
Volume	2
Issue number	5
DOIs	https://doi.org/10.1016/S1367-5931(98)80085-9
State	Published - Jan 1 1998

ASJC Scopus subject areas

Analytical Chemistry
Biochemistry

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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.",

author = "McLafferty, {Fred W.} and Kelleher, {Neil L.} and Begley, {Tadhg P.} and Fridriksson, {Einar K.} and Zubarev, {Roman A.} and Horn, {David M.}",

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AU - McLafferty, Fred W.

AU - Kelleher, Neil L.

AU - Begley, Tadhg P.

AU - Fridriksson, Einar K.

AU - Zubarev, Roman A.

AU - Horn, David M.

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AB - 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.

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