what proteins are present in complexes, using immunoprecipitation to find the protein–protein interactions. “It’s much easier” to analyze with LC/MS than with other techniques, he explains.
David’s proteomics core also uses the extraordinary sensitivity of LC/MS to undertake some less common structural analysis techniques, such as hydrogen-deuterium exchange, probing the sites where proteins are exposed to solvent.
David thinks that using LC/MS strictly for proteomics is “probably just the tip of the iceberg.” He points out that OHSU has a second core that does LC/MS only on small molecules—for example, to query small-molecule metabolites like adenosine triphosphate (ATP), phospholipids, or inter- mediates in purine metabolism. “And then we do all the protein analysis in our core.”
Reference 1. Basics of LC/MS Primer; Agilent Technologies, 2001; http://ccc.
chem.pitt.edu/wipf/Agilent%20LC-MS%20primer.pdf
Josh P. Roberts has been a full-time biomedical science writer for more than a decade. After earning an M.A. in the history and philosophy of sci- ence, he completed the Ph.D. program in molecular, cellular, developmen- tal biology, and genetics at the University of Minnesota, with dissertation research in ocular immunology; e-mail:
tcwriter@msn.com.
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www.americanlaboratory.com AMERICAN LABORATORY • 35 • JUNE/JULY 2013
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