Tamara Kinzer-Ursem

Dr. Kinzer-Ursem holds a bachelor’s degree in Bioengineering from the University of Toledo and Master and Ph.D. degrees in Chemical Engineering from the University of Michigan. Her postdoctoral training in Biology at Caltech focused on molecular neuroscience. She has also served as Head of Biochemistry Research and Development at a biotech firm in Monrovia, CA and Visiting Associate in Chemistry and Chemical Engineering at Caltech. She joined the faculty at Purdue University as Assistant Professor of Biomedical Engineering in  Spring of 2013.


Kinzer-Ursem T.L., Modeling G-Protein Coupled Receptors, In: Jaeger D., Jung R. (Ed.) Encyclopedia of Computational Neuroscience, SpringerReference: Springer-Verlag Berlin Heidelberg, In Press

Kulkarni, C., §Kinzer-Ursem T.L., §Tirrell, D.A.,  Selective Functionalization of the Protein N-Terminus with N-Myristoyl Transferase for Bioconjugation in Cell Lysate. (2013) Chembiochem, 14(15):1958-62

+Pepke S.L., +Kinzer-Ursem T.L., Mihalas S., Kennedy M.B. A dynamic model of interactions of Ca2+, calmodulin, and catalytic subunits of Ca2+/calmodulin-dependent protein kinase II. (2010) PLoS Computational Biology 6(2):e1000675.

Kinzer-Ursem, T.L., Linderman, J.J., Ligand- and cell-specific parameters affect ligand efficacy in a kinetic model of G protein coupled receptor signaling, (2007) PLoS Computational Biology, 3(1): e6.

Kinzer-Ursem, T.L. Sutton, K.L., Absood, A., Waller, A., Omann, G.M., Linderman, J.J., Multiple receptor states are required to describe both kinetic binding and activation of neutrophils via N-formyl peptide receptor ligand, (2006) Cellular Signaling, 18(10): 1732-47.

Waller, A., +Sutton, K.L., +Kinzer-Ursem, T.L., Absood, A., Traynor, J.R., Linderman, J.J., Omann, G.M., Receptor binding kinetics and cellular responses of six N-formyl peptide agonists in human neutrophils, Biochemistry, 43: 8204-8216.

+These authors contributed equally to this work

§ Co-Corresponding Author


BME 306 Biotransport Laboratory

Practical experience with fluid and mass transport principles is presented through inquiry-based laboratory modules. Each module contains computer simulations, experimental design, implementation, and data analysis. The lecture portion of this class is being run as a “flipped” classroom. Traditional lecture material is available online and class room time is dedicated to Q&A and working example problems relevant to the open ended laboratory modules.

BME 495/470  Biomolecular Engineering

This junior/senior level technical elective focuses on key concepts one needs to modify existing biomolecules, link biomolecules with other (bio)molecules, modify specific properties of biomolecules, and alter/enhance biomolecule functionality. Key physiochemical properties of nucleic acids, amino acids, lipids, and polysaccharides are reviewed in the first part of this course as well as the ways in which these molecule are detected and quantitatively measured. The second part of the course focuses on the application of biomolecular engineering to a variety of fields; tissue engineering, DNA-based materials, biosensors, etc. A project-based research proposal allows students to gain more depth of knowledge in a particular area of biomolecular engineering.

BME 405 Senior Design

This capstone design course provides students with hands on design experience in biomedical engineering. The primary objective is to engineer independent and original solutions to complex biomedical problems. Developed to mimic an industrial design experience; students establish design objectives and criteria, construct, test, analyze, iterate, and improve their design over the course of the semester. Project management, documentation, ethical considerations, and regulatory affairs topics facilitate the integration of professional and technical design skills into the design process.

BME 695 Critical Literature Analysis (CLA)

The Fall 2013 CLA class focused on literature surveying different methods that take advantage of protein post-translational modifications to site-specifically and selectively label proteins for a variety of biological and pharmaceutical applications.