University of Nebraska-Lincoln
634AA Hamilton Hall
Lincoln, NE 68588-0304
Our lab is a place where chemistry meets biology. The main focus of the group is on the study, modulation, and synthesis of a range of biologically important molecules including proteins, natural products, and artificial molecules. We are particularly interested in the elucidation of molecular mechanisms that are used by living organisms to achieve essential chemical transformations and the utilization of principles and tools of chemistry to manipulate biological processes.
Specific areas being explored include: (1) protein posttranslational modification (e.g., Protein tyrosine O-sulfation); (2) natural product biosynthesis; (3) small-molecule modulators of protein-protein interactions; and (4) chemo-biocatalytic syntheses. The goal of the research program is to use multidisciplinary and innovative approaches to tackle fundamental problems associated with human diseases and sustainable chemical production.
(1) Guo, J.; Melançon III, C. E.; Lee, H. S.; Groff, D.; Schultz, P. G. "Evolution of Amber Suppressor tRNAs for Efficient Bacterial Production of Unnatural Amino Acid-Containing Proteins" Angew. Chem. Int. Ed. Engl. 2009, 48, 9148-9151. [Link]
(2) Guo, J.; Wang, J.; Anderson, J. C.; Schultz, P. G. “Addition of an a-Hydroxy Acid to the Genetic Code of Bacteria” Angew. Chem. Int. Ed. 2008, 47, 722 –725. (This article was highlighted in Nature.) [Link]
(3) Guo, J.; Wang, J.; Lee, J. S.; Schultz, P. G. “Site-Specific Incorporation of Methyl- and Acetyl-Lysine Analogues into Recombinant Proteins” Angew. Chem. Int. Ed. 2008, 47, 6399–6401. (This article was highlighted in “Faculty of 1000 Biology”.) [Link]