We use of mass spectrometric methods for determining patterns of protein expression in biological systems. Effort is underway to develop proteomics methods and apply these to collaborations at BUMC and around the world. Active projects include: targeted proteomics for detecting cardiovascular disease and metabolic causes & Imaging mass spectrometry of brain tissue in neurological diseases

Involves the study of structural and functional aspects of protein glycosylation.  Many mammalian proteins contain glycan binding domains that interact with specific classes (known as epitopes) of glycoprotein glycans. The functions of glycoproteins, by virtue of the proteins to which they bind, depend heavily on context-depended glycans with which they are modified.  Effort is underway to develop and apply effective methods for glycoprotein analysis to meet the needs of biomedicine. Projects include: Top-down mass spectrometry of glycoproteins and clinically relevant protein & The roles of glycosylation in influenza A virus infectivity

We are studying of the structures and functions of glycans in biological systems. Glycans function in biomedicine according to the proteins (or protein domains) to which they bind. All cells are coated with a dense layer of glycans, through which all molecular interactions take place.  Effort is underway to develop and apply methods for analyzing glycans related to human disease questions.  Projects include: Glycomics of glycosaminoglycan, Elucidation of the glycan structures of methanogenic archaea, Identification of glycans in human milk that are protective against HIV infection, Activated electron dissociation tandem mass spectrometry of glycans, Development of software for interpretation of glycan mass spectra

Faculty conducting research in these areas