Robert Weis

Associate Professor, Dept. of Chemistry
602 Lederle GRT, University of Massachusetts
Amherst, MA 01003-9292
(413) 545-0464
rmweis@chem.umass.edu
http://www.chem.umass.edu/Faculty/weis.htm
Functional Assemblies of Biological Macromolecules
Biological macromolecules are the building blocks of cellular nanomachines involved in a diverse array of functions including chemical synthesis, sensing, and force generation. Our interests are to understand the organization and function of protein complexes involved in chemical sensing by bacterial cells. With the developing picture of this fundamental process, we are able to re-engineer the structural and functional properties of these proteins for applications that use biomaterials in nanotechnological applications.
| Research Interest | Potential Application |
|---|---|
| The structure and function of biological membranes including transmembrane signaling mechanisms | The development of chemical sensing modules based on protein assemblies for use in integrated sensors |
| Fundamental properties of template-directed assembly of protein complexes, particularly proteins involved in cellular signaling pathways | Utilization of template-directed assembly methods for robust and efficient screens of biological function |
Honors and Awards
- Lilly Teaching Fellowship , 1995
- Arnold & Mabel Beckman Young Investigator Award, 1992
Publications
- Lefman, J., P. Zhang, T. Hirai, R. M. Weis, J. Juliani, D. Bliss, M. Kessel, E. Bos, P. Peters, and S. Subramaniam. 2004. 3D electron microscopic imaging of membrane invaginations in E. coli overproducing the chemotaxis receptor Tsr. J. Bacteriol. (in press).
- Shrout, T. S., D. J. Montefusco, and R. M. Weis. 2003. Template-directed assembly of receptor signaling complexes. Biochemistry 42, 13379-13385.
- Weis, R. M., T. Hirai, A. Chalah, M. Kessel, P. Peters, and S. Subramaniam. 2003. Structural analysis and cellular tomography of the bacterial chemotaxis receptor Tsr. J. Bacteriol. 185, 28-35.
- Li, G., and R. M. Weis. 2000. Covalent modification regulates ligand binding to receptor complexes in the chemosensory system of Escherichia coli. Cell 100, 357–365.
- Rao., J, J. Lahiri, R. M. Weis and G. M. Whitesides. 2000. Design, synthesis, and characterization of a high-affinity trivalent system derived from vancomycin and l-lys-d-ala-d-ala. J Amer. Chem. Soc. 122, 2698-2710.


