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Protein arrays via mass spec Using tandem mass spectrometry and "soft-landing" collection, chemistry professor R. Graham Cooks and coworkers at Purdue University have devised a novel way to create protein microarrays [Science, published Aug. 14, http://www.sciencemag.org/cgi/content/abstract/1088776.v1]. Although there are other methods of depositing macromolecules onto solid supports, the team's approach combines protein separation and surface deposition in one step. Using mass spectrometry to separate the components dramatically reduces the time it takes to create the array and provides a highly selective means to separate proteins with similar structures. When Cooks's team made both trypsin and lysozyme arrays using their soft-landing method, they found that the enzymes retained virtually all of their biological activity under the experimental conditions. More delicate enzymes, such as yeast hexokinase, also survived the ionization, mass selection, and soft-landing processes intact but only retained activity when they were propelled into hydrophilic solutions rather than onto solid surfaces |
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