Two-dimensional mass spectrometry of biomolecules at the subfemtomole level. Academic Article

abstract

• Multiple dimensions of unique molecular structure information can now be obtained from proteins and DNA using mass spectrometry. Less than 10(-16) 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 (> 10(5) and 10(-17) mol sensitivity of Fourier-transform mass spectrometry provide exact molecular weight values (+/- 1 or 2 Da) for mixture components, indicating error 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.

authors

• Begley, Tadhg

published proceedings

• Curr Opin Chem Biol

author list (cited authors)

• McLafferty, F. W., Kelleher, N. L., Begley, T. P., Fridriksson, E. K., Zubarev, R. A., & Horn, D. M.

citation count

• 37

complete list of authors

• McLafferty, FW||Kelleher, NL||Begley, TP||Fridriksson, EK||Zubarev, RA||Horn, DM

publication date

• January 1998

publisher

• Elsevier  Publisher

published in

• Current Opinion in Chemical Biology  Journal

keywords

• Alkyl And Aryl Transferases
• Animals
• Base Sequence
• Carbonic Anhydrases
• Cattle
• Cytochrome C Group
• DNA
• Fourier Analysis
• Gas Chromatography-Mass Spectrometry
• Horses
• Major Histocompatibility Complex
• Molecular Weight
• Protein Conformation
• Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
• Thiamine
• Ubiquitins

Digital Object Identifier (DOI)

• 10.1016/s1367-5931(98)80085-9

start page

• 571

end page

• 578

volume

• 2

issue

• 5

URL

• http%3A%2F%2Fdx.doi.org%2F10.1016%2Fs1367-5931%2898%2980085-9