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 - 1998

Funding

We thank Barbara Baird, Barry Carpenter, H Floyd Davis, Yuan Gao, Albert Heck, Franz Hillenkamp, Donald Hunt, Nathan Kruger, David Holowka, Petia Shipkova and Evan Williams for valuable discussions and/or measurements, the National Institutes of Health (grant number GM16609 to FW McLafferty; DK44083 to TP Begley, and Training Grant number 08-T2GM07273 to NL Kelleher) and the American Chemical Society Division of Analytical Chemistry (a full fellowship, sponsored by Perkin-Elmer Corp \[NL Kelleher\]) for generous funding.

ASJC Scopus subject areas

Analytical Chemistry
Biochemistry

Access to Document

10.1016/S1367-5931(98)80085-9

Cite this

@article{b4e8db50f1a24eacb2db3d65fd973891,

title = "Two-dimensional mass spectrometry of biomolecules at the subfemtomole level",

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.}",

note = "Funding Information: We thank Barbara Baird, Barry Carpenter, H Floyd Davis, Yuan Gao, Albert Heck, Franz Hillenkamp, Donald Hunt, Nathan Kruger, David Holowka, Petia Shipkova and Evan Williams for valuable discussions and/or measurements, the National Institutes of Health (grant number GM16609 to FW McLafferty; DK44083 to TP Begley, and Training Grant number 08-T2GM07273 to NL Kelleher) and the American Chemical Society Division of Analytical Chemistry (a full fellowship, sponsored by Perkin-Elmer Corp \[NL Kelleher\]) for generous funding.",

year = "1998",

doi = "10.1016/S1367-5931(98)80085-9",

language = "English (US)",

volume = "2",

pages = "571--578",

journal = "Current Opinion in Chemical Biology",

issn = "1367-5931",

publisher = "Elsevier Ltd",

number = "5",

}

TY - JOUR

T1 - Two-dimensional mass spectrometry of biomolecules at the subfemtomole level

AU - McLafferty, Fred W.

AU - Kelleher, Neil L.

AU - Begley, Tadhg P.

AU - Fridriksson, Einar K.

AU - Zubarev, Roman A.

AU - Horn, David M.

N1 - Funding Information: We thank Barbara Baird, Barry Carpenter, H Floyd Davis, Yuan Gao, Albert Heck, Franz Hillenkamp, Donald Hunt, Nathan Kruger, David Holowka, Petia Shipkova and Evan Williams for valuable discussions and/or measurements, the National Institutes of Health (grant number GM16609 to FW McLafferty; DK44083 to TP Begley, and Training Grant number 08-T2GM07273 to NL Kelleher) and the American Chemical Society Division of Analytical Chemistry (a full fellowship, sponsored by Perkin-Elmer Corp \[NL Kelleher\]) for generous funding.

PY - 1998

Y1 - 1998

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=0032176802&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032176802&partnerID=8YFLogxK

U2 - 10.1016/S1367-5931(98)80085-9

DO - 10.1016/S1367-5931(98)80085-9

M3 - Article

C2 - 9818181

AN - SCOPUS:0032176802

SN - 1367-5931

VL - 2

SP - 571

EP - 578

JO - Current Opinion in Chemical Biology

JF - Current Opinion in Chemical Biology

IS - 5

ER -

Two-dimensional mass spectrometry of biomolecules at the subfemtomole level

Abstract

Funding

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this