Dr. Benjamin Jennings joins the Department of Medicine
November 30, 2018
Dr. Benjamin Jennings joined the Department of Medicine as an Instructor in the Division of Hematology in October, 2018.
Dr. Jennings is a strong bench scientist with experience determining molecular and enzymatic mechanisms. He has experience while at the University of Michigan included specializing in molecular mechanisms, enzymology, regulation and trafficking consequences of protein post-translational modifications. He has extensive experience in protein expression, purification and quantitative characterization and he has published a first author paper using kinetics to map binding sites that explains the substrate differences between two related enzymes. He also used biochemical assays to determine how a pair of shuttling chaperone proteins regulate the modification, trafficking and enzymatic activity of several oncogenetic small GTPases, used steady-state kinetics and mutagenesis to pap residues in acetyltransferases responsible for binding and resistance in disease-causing bacteria. He has executed and problem-solved experiments, collected and analyzed results, including derivation of non-standard binding and reaction equations. He also developed valuable skills through teaching and coordinating courses in chemistry. In addition, Dr. Jennings designed, cloned and mutated plasmids; optimized bacterial expressions, including codon usage and co-expressions with folding chaperones and binding partners; purified proteins using FPLC and gravity-based chromatography; verified constructs by mass spectrometry, western blotting, and SDS-PAGE; and quantified enzyme concentrations by active site titrations.
His scholarly and research focus at Washington University School of Medicine will be to study the underlying mechanisms for the trafficking of GlcNac-1-phosphotransferase and other Golgi glycosyltransferases. He will continue studies to uncover the role of the various domains of GlcNAc-1-phosphotransferase in the recognition and selective phosphorylation of lysosomal enzymes.Categories: Announcements