Current Projects:

We study the basis of protein stability and the formation of protein complexes in vivo using a combination of high-throughput methods, bioinformatics and chemical biology tools.  Key methods that we use in the lab include protein engineering and biophysical characterization, combinatorial chemistry, statistical analysis, and unnatural amino acid mutagenesis.  We also apply these technologies for the improvement of protein therapeutics.

Five Recent Publications:

• Sullivan BJ, Durani V, Magliery TJ. Triosephosphate isomerase by consensus design: dramatic differences in physical properties and activity of related variants. J Mol Biol. 2011, 413, 195.
• Magliery TJ, Lavinder JJ, Sullivan BJ. Protein stability by number: high-throughput and statistical approaches to one of protein science's most difficult problems. Curr Opin Chem Biol. 2011, 15, 443.
• Nie L, Lavinder JJ, Sarkar M, Stephany K, Magliery TJ. Synthetic approach to stop-codon scanning mutagenesis. J Am Chem Soc. 2011, 133, 6177.
• Hari SB, Byeon C, Lavinder JJ, Magliery TJ. Cysteine-free Rop: a four-helix bundle core mutant has wild-type stability and structure but dramatically different unfolding kinetics. Protein Sci. 2010, 19, 670.
• Otto TC, Harsch CK, Yeung DT, Magliery TJ, Cerasoli DM, Lenz DE. Dramatic differences in organophosphorus hydrolase activity between human and chimeric recombinant mammalian paraoxonase-1 enzymes. Biochemistry, 2009, 48, 10416.

Publication at PubMed