Biological Mass Spectrometry and Proteomics Laboratory
The Biological Mass Spectrometry Laboratory functions as both a core and an independent research facility. Its focus is the structural characterization of peptides and proteins, especially post-translational modifications, at the low picomole/high femtomole level. Wadsworth Center researchers employ the Laboratory routinely to: verify the integrity/fidelity of recombinant proteins, determine the molecular weight distribution and composition of oligosaccharides, determine the products of organic reactions, as well as other applications. These routine services provide important quality assurance for ongoing public health-related research studies. Collaborative projects are also undertaken to identify unknown proteins and peptides, characterize their properties, and determine post-translational modifications such as phosphorylation and glycosylation on a nominal fee-for-service basis. The Laboratory's efforts include biomolecule MS and proteomic methods development.
Ion trap - microelectrospray mass spectrometry is performed on a ThermoFinnigan LCQ Deca MS. This instrument is coupled to a 75-micron i.d. reverse-phase chromatography system to acquire picomole protein digest/peptide molecular weight maps and MS/MS spectra. Protein identification and post-translational modifications are determined by querying the appropriate DNA/protein database with MS/MS spectra using the SEQUEST database search computer program.
Ion trap - nanoelectrospray mass spectrometry is performed on a ThermoFinnigan LTQ MS. This instrument is coupled to a Dionex Ultimate-3000 nanochromatography system to automatically acquire femtomole protein digest/peptide molecular weight maps and MSn spectra. Protein identification and post-translational modifications are determined by querying the appropriate DNA/protein database with MS/MS spectra using the Turbo SEQUEST database search computer program.
The MS core incorporates a full complement of Bio-Rad proteomic 1D and 2D gel electrophoresis equipment and PDQuest software for gel analysis, comparison, and database searching, all situated in a dedicated facility. This suite of equipment is used in conjunction with the mass spectrometers to determine protein identification by offering gel separations and in-gel proteolytic digest service. For larger projects beyond the "proof-of-concept" stage of development, the proteomic core staff provides hands-on training and support using the core's instrumentation.
Contact:
hauer@wadsworth.org (518) 486-4913
Dr. Charles Hauer III, Director.
Mr. Robert Stack, Mass Spectroscopist and Facility Manager