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Core Director

Robert N. Cole, Ph.D. is the Director of the Mass Spectrometry and Proteomics Facility at Johns Hopkins University School of Medicine (JHU SOM). Dr. Cole has 20 years of experience using protein biochemistry and mass spectrometry to identify proteins and map post-translational modifications. He has peer-reviewed publications related to acetylation, glycosylation, nitrosation, or phosphorylation post-translational modifications and novel clevage sites, and has co-authored several book chapters, including “Current Protocols in Protein Science and Mass Spectrometry in Biology and Medicine”. He has Co-Chaired the Greater Baltimore-Washington Area Mass Spectrometry Discussion Group, as well as proteomic sessions at scientific meetings. In 2000, Dr. Cole established this open access mass spectrometry facility. The facility has grown in personnel, equipment and space to include gel- and column-based quantitative proteomic techniques and offers workshops in protein identification, gel electrophoresis and mass spectrometry-based proteomic techniques. 

Proteomics Specialists

Tatiana Boronia, Ph.D. has over 10 years experience with MALDI, tandem MS and proteomic analyses of proteins, peptides and small molecules. She was trained in analytical chemistry at Moscow State University and post-doctoral trained in proteomics with Dr. Robert Fisher at the Protein Chemistry Laboratory, SAIC-Frederick, MD. She developed a highly sensitive ion mapping technique for identifying phosphorylated or O-GlcNAc modified peptides. She adapted the iTRAQ method for quantifying proteins to identifying and quantifying posttranslational modifications from proteins in gel bands. Dr. Boronia also instructs and advises Hopkins investigators in the use of the Core’s MALDI-TOF mass spectrometer. 

Lauren DeVine, MS. has over 8 years experience in protein biochemistry, including sample preparation, 2-D gel electrophoresis, chromatography (TLC, affinity and HPLC), protein and phosphorylation and quantification by tandem MS, DIGE or iTRAQ/Tandem Mass Tag analysis. Mrs. DeVine also processes biological samples, including HPLC depletion of serum, plasma and urine for proteomics experiments. She was trained in environmental proteomics at California State University, San Luis Obispo where she studied the proteomic response of Pacific oysters to reactive nitrogen stress. Mrs. DeVine instructs and advises Hopkins investigators in the use of the Core’s gel electrophoresis and imaging equipment, MALDI and nanospray mass spectrometers. 

Robert N. O’Meally, M.S. has over 10 years experience as a research chemist in environmental and biotechnology fields and 7 years experience in proteomic analyses. He was trained in analytical chemistry at University of Maryland, College Park. Mr. O’Meally has developed liquid chromatography and MS based methods for analyzing small molecules, oligonucleotides, proteins and protein modifications from environmental and biological samples. He developed assays for: high resolution mass analysis of intact proteins from complex mixtures; mapping and quantifying nitrosation and phosphorylation sites; quantifying oxidative damage to DNA; and determining fatty acid composition. He has extensive hands-on experience with many mass spectrometers including ion traps and orbitraps (ThermoFisher Orbitrap Velos, Orbitrap XL, LCQ, LTQ XL and Agilent/Bruker), triple quadrupoles (ThermoFisher TSQ Vantage, PE Sciex API 3000 and 150EX), orthogonal-TOFs (AB Sciex and Burker), gas chromatographs (Agilent, Perkin Elmer, Fisons) and most HPLC systems (Agilent, Beckman, Dionex, Eksigent, Shimadzu, Waters). Mr. O’Meally instructs and advises investigators on chromatography and nanospray mass spectrometry applications.

Simion D. Kreimer, Ph.D. has over 5 years experience developing novel data acquisition and analysis strategies for identifying proteins by mass spectrometry. He was trained in analytical biochemistry by Dr. Barry Karger at Northeastern University. He has designed and automated targeted and untargeted data independent acquisition (DIA) methods to identify low abundance proteins present and potentially contaminating highly purified and concentrated proteins. He has applied this workflow to antibodies, recombinant purified proteins and to identifying proteins in plasma-derived extracellular. He is proficient in discovery and targeted proteomic analysis software (Proteome Discoverer, PEAKS, MaxQuan, and SearchGUI) and has developed and maintained spectral libraries using SpectraST and Skyline.  He has hands on experience maintaining and operating Thermo Orbitrap mass spectrometers and most HPLC systems operated (Eksigent 2D nano-LC, Dionex Ultimate 3000 and 3500) at nanoflow (200-300 nL/min) and ultra-low flow (10-20 nL/min) rates. Dr. Kreimer assists investigators with designing their quantitative proteomic experiments, sample preparation and customizing their MS analysis to meet the project goals.

 

 

Location

The Johns Hopkins Mass Spectrometry and Proteomic Facility

725 N. Wolfe Street
Wood Basic Science Building, Room 504
Baltimore, MD 21205

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