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Our lab is characterizing the S. solfataricus proteome by estabishing
the protein composition of wild type and targeted disruption mutant
strains. Two dimensional SDS PAGE of total protein extracts separates
proteins based on mass and charge. Selected proteins are Trypsin
hydrolyzed and the resulting peptides fractionated by capillary
electrophoresis. Appropriate peptides are identified by tandem mass
spectrometry (MS/MS) followed by matching to the S. solfataricus
sequenced genome.

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