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Analytical Chemistry

Mass Spec Anniversary

February 9, 2009 | A version of this story appeared in Volume 87, Issue 6

THE 50TH ANNIVERSARY of the first application of mass spectrometry (MS) to the analysis of amino acids and peptides appears to have largely gone unnoticed by current-day practitioners in the "omics" areas.

I recommend Carl-Ove Anderson's article to those interested in the history of biological mass spectrometry (Acta. Chem. Scand. 1958, 12, 1353). This paper is remarkable for several reasons: It is short (less than half a page), shows not a single figure, correctly highlights the main fragment ions observed in the electron ionization/MS of methyl esters as being due to the formation of H2NCHR+ and H2NCHCO2CH3+ ions, and recognizes the then-limitations of electron ionization/MS analysis by highlighting the need to derivatize peptides via N and C terminal protection.

In the intervening half century, growth in MS-based analysis of biological molecules has been explosive and largely fueled by instrumental developments ranging from the invention of new ionization techniques (recall the Nobel Prizes for electrospray ionization and matrix-assisted laser desorption/ionization), the introduction of tandem mass spectrometry, and the use of computers to control mass spectrometers and acquire data.

Indeed, the sequencing of peptides
by mass spectrometry has evolved from being a curious potential rival of chemical methods, such as Edman sequencing, to becoming one of the cornerstones of proteomics.

Richard A. J. O'Hair
Victoria, Australia


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