Prof. Hui Zhang
The Johns Hopkins University School of Medicine
Time：2015.3.11 (Wednesday) 9:30am
Location: 406 Room, Biotechnology Division, Dalian Institute of Chemical Physics
Introduction：
Education and Training (in chronological order):
1989 B.S. Plant Biochemistry, Beijing University, Beijing, China.
1992 M.S. Gene and Protein Engineering, Beijing University, Beijing, China.
1999 PhD Biochemistry, University of Pennsylvania, Philadelphia, PA.
Professional Experience (in chronological order):
1998-1999 Product Manager, New England Biolabs, Beverly, MA.
1999-2001 Scientist and Senior Scientist, Cell Signaling Technology, Beverly, MA.
2001-2003 Research Scientist, Institute for Systems Biology, Seattle, WA.
2003-2006 Senior Research Scientist, Institute for Systems Biology, Seattle, WA.
2006-2011 Assistant Professor, Department of Pathology, Johns Hopkins University, Baltimore, MD.
2011-present Associate Professor, Department of Pathology, Johns Hopkins University, Baltimore, MD.
2012-present Director of Mass Spectrometry Core Facility, Center for Biomarker Discovery and Translation. Johns Hopkins University, Baltimore, MD
Abstract：
Protein glycosylation is one of the most common forms of protein modifications. Each glycoprotein can be glycosylated at different glycosites and each glycosite may be modified by different glycans. This structural heterogeneity provides additional functions for each glycoprotein in physiological and pathological processes. However, the structural heterogeneity also complicates the studies of structure-function relationships of glycoproteins. To rapidly identify and quantify the glycosylation on each glycosite from complex biological mixtures and to understand the function of protein glycosylation, we developed an integrated approach for global proteomics, glycoproteomics, and glycomics, with which peptides and glycans are isolated and separated by liquid-chromatography followed by quantitative analysis by mass spectrometry. When we performed integrated quantitative analyses to determine protein abundance, glycosylation site occupancy and glycan structures, we showed by specific examples that upon the identification of glycoproteins, glycosites containing specific glycans were readily identifiable and quantifiable. The applications of integrated approach to biological problems facilitate the understanding of glycosylated forms in cellular functions.
Contact：1809 Group Prof. Mingliang Ye （9620）