TuKiet Lam, PhD, BS

I am the Director of the Keck MS & Proteomics Resource at the Yale School of Medicine and have been with Yale since 2004. My specific aims are to train, assist, collaborate, and make available my expertise in mass spectrometry to as many investigators of other scientific and biomedical discipline as possible so that they can advance their research. By establishing a well-organized and well-trained core group of staff who are dedicated to the same philosophy and mission, my team provides the high-quality mass spectrometry data and analyses which have resulted in co-authorships and acknowledgements in many high impact scientific publications. My mass spectrometry (MS) footing grew from my graduate career at Florida State University, where I developed a hydrogen/deuterium exchange workflow to robustly observe protein-protein interaction(s) and structural changes in proteins. The technique led to the discovery of unique conformational changes in HIV-1 viral capsid protein (Lanman, et. al., JMB, 325, 759-772, 2003, Cover). I became involved in many collaborative projects during my postdoctoral work at the National High Magnetic Field Lab and began to shape my career in using my analytical chemistry skillsets in high resolution tandem mass spectrometry to work with a multitude of investigators across many basic scientific and applied biomedical disciplines to understand biological functions at the molecular level. My successful multidisciplinary collaborative interaction with these investigators falls in the areas of protein identification, profiling, and quantitation; protein posttranslational modification (PTM); protein-protein interactions; natural products; metabolites; green chemistry; and organic product syntheses among many others. During my residence within the Keck MS and Proteomics Resource, I collaborated with many biomedical and clinical investigators in their aims to better understand protein(s) functions in various relevant disease and cancers studies such as illustrated in Fogel et al, 2010, (which was featured on the cover of J. Biol. Chem. 285, 34864); Musante et al, 2017 (Elife 6); Miller et al, 2017 (ACS Chem Neurosci, 8(7), 1554); Sun et al, 2016 (Arthritis Rheumatology, 68(5), 1252); Tellez et al, 2013 (Sciene 341(6147), 800); Klein et al, 2017 (Neruon 95, p281); Goffredo et al, 2017 (Nutrients, 9, p 642); and Henderson et al, 2016 (Acta Neuropathol 131, p621). Currently I am involved in many projects which utilizes high resolution tandem mass spectrometry (Orbitrap family of mass spectrometers) along with various labeled and label free methodologies for protein ID/profiling and quantitation in various biological systems (i.e. brain, serum, plasma, liver, endothelial cells, FACS sorted cells, neurons, worms, mosquitos, flies, etc.), for protein posttranslational modification (e.g. ubiquitinylation, palmitoylation, acetylation, and phosphorylation), for small molecule quantitation and structural elucidation (e.g. targeted metabolite quantitation, pharmacokinetics study of drug metabolism, controlled substance efficacy assays, etc.). The use of these exceedingly more reproducible high resolution tandem mass spectrometry technologies to facilitate protein and protein posttranslational modification ID and quantitative global profiling provides a very robust and biostatistical confident way to monitor proteins and small molecules changes, functions, and interactions within a complex biological system.