Understanding complex biological systems demand novel tools allowing the investigator to probe and manipulate its specific components. One major focus of our group is the development and application of methods enabling site-specific labeling of any chosen protein in a living cell with useful biochemical and biophysical probes to investigate its function in its native environment. Another focus of our group is developing proteins with novel functions by rational and directed evolution. We are also interested in augmenting the functional potential of proteins by introducing new chemical moieties within the canonical protein-scaffold. Research in our group combines elements from a diverse set of disciplines spanning synthetic chemistry, biochemistry, molecular biology and cell biology.
Representative Key Publications:
“A Tryptophanyl-tRNA Synthetase/tRNA Pair for Unnatural Amino Acid Mutagenesis in E. coli,” A. Chatterjee*, H. Xiao*, P.Y. Yang, G. Soundararajan, P.G. Schultz. Angew Chem Int Ed Engl. 2013
, doi: 10.1002/anie.201301094.
“Evolution of multiple, mutually orthogonal prolyl-tRNA synthetase/tRNA pairs for unnatural amino acid mutagenesis in Escherichia coli,” A. Chatterjee*, H. Xiao*, P.G. Schultz. Proc Natl Acad Sci U S A. 2012
“Saccharomyces cerevisiae THI4p is a suicide thiamine thiazole synthase,” A. Chatterjee, N.D. Abeydeera, S. Bale, P.J. Pai, P.C. Dorrestein, D.H. Russell, S.E. Ealick, T.P. Begley. Nature
“Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily,” A. Chatterjee*, Y. Li*, Y. Zhang, T.L. Grove, M. Lee, C. Krebs, S.J. Booker, T.P. Begley, S.E. Ealick. Nat Chem Biol. 2008, 4, 758-65.
“Biosynthesis of thiamin thiazole in eukaryotes: conversion of NAD to an advanced intermediate,” A. Chatterjee, C.T. Jurgenson, F.C. Schroeder, S.E. Ealick, T.P. Begley. J Am Chem Soc. 2007, 129, 2914-22.
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