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) |
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Pages (from-to) | 571-578 |
Number of pages | 8 |
Journal | Current Opinion in Chemical Biology |
Volume | 2 |
Issue number | 5 |
DOIs | |
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