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In vitro and cell-based evolution of novel protein function

Many of our imaging technologies are based on engineered proteins, and thus we rely heavily upon protein engineering techniques. In vitro evolution is a powerful method to engineer novel protein function, yet common methods such as phage display are best for evolving new binding function, rather than new catalytic function. We are interested in developing fundamentally new in vitro and cell-based evolution strategies, that can be used by any lab to evolve new catalytic activity for any protein of interest. Our metric for success will be the ability to enrich, from a large pool of enzyme variants, highly active species over moderately active ones.

Related publications:  

Yeast display evolution of a kinetically-efficient 13-amino acid substrate for lipoic acid ligase.
Journal of the American Chemical Society 2009, 131, 16430-16438.
S. Puthenveetil, D. S. Liu, K. A. White, S. Thompson, and A. Y. Ting.

Phage display evolution of a peptide substrate for yeast biotin ligase and application to two-color quantum dot labeling of cell surface proteins.
Journal of the American Chemical Society 2007, 129, 6619-6625.
I. Chen, Y.-A. Choi, and A. Y. Ting.

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