The overall goal of our laboratory is to characterize the structure/function relationships of a variety of enzymatic catalysts at the atomic level. Much of this work is being extended into efforts to engineer novel structures and properties onto existing protein and enzyme scaffolds. A unifying theme between many of the individual projects is the selection and engineering of these enzymes for targeted therapeutic and/or biotech/industrical applications.
The tools employed by our lab are X-ray crystallography, computer modeling, and genetic manipulation of the molecules of interest, combined with biochemical analyses of function.
Ennist NM, Wang S, Kennedy MA, et al. Stoddard BL, Romero E, Hunter CN, Baker D. " De novo design of proteins housing excitonically coupled chlorophyll special pairs" (2024) Nat Chem Biol. 20 (7):906-915. doi: 10.1038/s41589-024-01626-0. PMID: 38831036; PMCID: PMC11213709.
Kibler RD, Lee S, Kennedy MA, Wicky BIM, Lai SM, Kostelic MM, Carr A, Li X, Chow CM, Nguyen TK, Carter L, Wysocki VH, Stoddard BL, Baker D. Design of pseudosymmetric protein hetero-oligomers. Nat Commun. 2024 Dec 18;15(1):10684. doi: 10.1038/s41467-024-54913-8. PMID: 39695145; PMCID: PMC11655659.
Lee S, Kibler RD, Ahn G, Hsia Y, Borst AJ, Philomin A, Kennedy MA, Huang B, Stoddard B, Baker D. Four-component protein nanocages designed by programmed symmetry breaking. Nature. 2024 Dec 18. doi: 10.1038/s41586-024-07814-1. Epub ahead of print. PMID: 39695226.