Directory: Faculty
 |
Kenneth WoycechowskyBIOLOGICAL CHEMISTRYAssistant Professor B.S. Pennsylvania State University, 1994 Phone: (801) 587-9973 Office: HEB 1320 Email: kwoycech@chem.utah.edu |
Activities & Awards
- NIH Ruth L. Kirschstein National Research Service Award, 2004-2006
- NIH Chemistry-Biology Interface Training Grant, 1995-1998
- Wisconsin Alumni Research Foundation Fellowship, 1994-1995
- Penn State University Scholars Program, 1990-1994
Research Interests
Our research program aims at a deeper understanding of the chemical and biological properties of proteins and enzymes. We take an engineering approach, using the biopolymers found in nature as starting points for the generation of variants with interesting properties. In turn, the detailed characterization of the novel proteins generated in our lab will provide insight into the general principles that govern structure-function relationships in biological systems.
We focus on the (often inter-related) processes of protein folding, assembly, and function. Through judicious application of rational or random mutagenesis, collections of amino acid sequences are generated and then subjected to screens or selections to identify those that meet specific structural/functional criteria. Initial efforts address the following issues: 1) the role of specificity in self-assembly (with an emphasis on amyloid fibrillization and the formation of virus-like capsids), 2) the pathways by which proteins can evolve, and 3) the development of novel enzymes, receptors, drug delivery systems, and biomaterials.
The research carried out in our laboratory provides training at the interface of chemistry and biology. Understanding the chemical biology of proteins requires a variety of experimental approaches, including biochemistry, organic chemistry, biophysics, microbiology, and molecular biology. The combination of diverse techniques can help us elucidate a more sophisticated view of how proteins and enzymes work. The knowledge gained can then be exploited to generate customized catalysts, sensors, or molecular machines for myriad applications in industry and medicine.
Selected Publications
- K. J. Woycechowsky, A. Choutko, K. Vamvaca, and D. Hilvert “Mutational robustness of an enzymatic molten globule compared to its thermostable counterpart” 2008, submitted.
- J. Beld, K .J. Woycechowsky, and D. Hilvert “Catalysis of oxidative protein folding by small-molecule diselenides” Biochemistry 2008, 47, 6985–6987.
- M. Toscano, K.J. Woycechowsky, and D. Hilvert “Minimalist active-site redesign: teaching old enzymes new tricks” Angew. Chem. Int. Ed. 2007, 46, 3212-3236.
- K. J. Woycechowsky, K. Vamvaca, and D. Hilvert “Novel enzymes through design and evolution” Adv. Enzymol. Relat. Areas Mol. Biol. 2007, 75, 241-294.
- K. J. Woycechowsky, F.P. Seebeck, and D. Hilvert “Tunnel plasticity and quaternary structural integrity of a pentameric protein ring” Protein Sci. 2006, 15, 1106-1114.
- F. P. Seebeck, K.J. Woycechowsky, W. Zhuang, J. Rabe, and D. Hilvert “A simple tagging system for protein encapsulation” J. Am. Chem. Soc. 2006, 128, 4516-4517.
- K. J. Woycechowsky and R. T. Raines “The CXC motif: a functional mimic of protein disulfide isomerase” Biochemistry 2003, 42, 5387-5394.
- K. J. Woycechowsky, K.D. Wittrup, and R.T. Raines “A small-molecule catalyst of protein folding in vitro and in vivo” Chem. Biol. 1999, 6, 871-879.