Kenneth J. Woycechowsky, Ph.D.

Affiliations: 
2002 University of Wisconsin, Madison, Madison, WI 
Area:
Chemical biology, protein design and engineering, enzymology, biofuels
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"Kenneth Woycechowsky"

Parents

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Ronald T. Raines grad student 2002 UW Madison
 (Small-molecule catalysis of native disulfide bond formation in proteins)
Donald M. Hilvert post-doc ETH/Uni Zurich (Chemistry Tree)
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Publications

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Lilavivat S, Sardar D, Jana S, et al. (2012) In vivo encapsulation of nucleic acids using an engineered nonviral protein capsid. Journal of the American Chemical Society. 134: 13152-5
Chen HN, Woycechowsky KJ. (2012) Conversion of a dodecahedral protein capsid into pentamers via minimal point mutations. Biochemistry. 51: 4704-12
Steiner AM, Woycechowsky KJ, Olivera BM, et al. (2012) Reagentless oxidative folding of disulfide-rich peptides catalyzed by an intramolecular diselenide. Angewandte Chemie (International Ed. in English). 51: 5580-4
Wörsdörfer B, Woycechowsky KJ, Hilvert D. (2011) Directed evolution of a protein container. Science (New York, N.Y.). 331: 589-92
Beld J, Woycechowsky KJ, Hilvert D. (2010) Diselenides as universal oxidative folding catalysts of diverse proteins. Journal of Biotechnology. 150: 481-9
Beld J, Woycechowsky KJ, Hilvert D. (2010) Small-molecule diselenides catalyze oxidative protein folding in vivo. Acs Chemical Biology. 5: 177-82
Beld J, Woycechowsky KJ, Hilvert D. (2009) Selenoglutathione: Efficient oxidative protein folding by a diselenide (Biochemistry (2007), 46, 18, (5382-5390)) Biochemistry. 48: 4662
Woycechowsky KJ, Choutko A, Vamvaca K, et al. (2008) Relative tolerance of an enzymatic molten globule and its thermostable counterpart to point mutation. Biochemistry. 47: 13489-96
Beld J, Woycechowsky KJ, Hilvert D. (2008) Catalysis of oxidative protein folding by small-molecule diselenides. Biochemistry. 47: 6985-7
Toscano MD, Woycechowsky KJ, Hilvert D. (2007) Minimalist active-site redesign: teaching old enzymes new tricks. Angewandte Chemie (International Ed. in English). 46: 3212-36
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