Mass Spectrometry Of Drugs, Natural Products, Proteins,

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The research of this unit has moved over the last year to almost entirely proteome research. The group identifies disulfide bonds and other post-translational modifications in proteins that are part of collaborative research. Method improvement and development are important aspects of the group's emphasis. Over the past year, a new Q-TOF mass spectrometer has been acquired by the laboratory and this was a collaborative purchase between NIDDK and four other institutes. Its use is shared between the collaborating institutes. Booking for the instrument and the data are all made available online so the remote researchers can process their data and must only come to the laboratory to insert their samples. This is sharing of the resource is proving highly successful. A gel digestion station was also added for larger scale digestion and identification of proteins that vary in abundance between a normal and diseased state. While using gels to identify these proteins is a useful approach, an emphasis in the group's development work has been in methods for doing these analyses on the whole proteome from a cell system. Major research projects within the group have involved the determination of post-translational modifications in very large and complex proteins, methods for the analysis and identification of hydrophobic proteins, the identification of unusual/modified amino acids in biologically active peptides, development of cross-linking method to elucidate 3-D structures of proteins and proteins interactions, the characterization of novel annexins, and the identification of an in-vivo modification of S-adenosylmethionine decarboxylases. A very close collaboration is maintained with the Laboratory of Biophysical Chemistry, NHLBI.