Metalloprotein Design

Metalloprotein Design and Evolution

Metal ions and metal-bound cofactors are ubiquitous in natural protein and protein complexes, typically as centers for enzymatic catalysis. Research in the metalloprotein subgroup focuses on the elucidation and development of design rules for the rational engineering of metalloprotein oligomers which utilize metal ions to drive self-assembly and access novel catalytic or electron transfer capabilities. Such attractive functionalities are the consequence of complex relationships between protein structure, inorganic reactivity, biochemistry, and redox chemistry. We have previously reported supramolecular architectures with in vivo catalytic activities and allosteric behavior. Current efforts are focused on diversifying the structures and functions of such architectures and expanding their scope beyond the biologically available metal ions.

Principal members: Eyal, Julian, Albert, Francis
Affiliated members: Rob
 

Selected Publications

 


L.A. Churchfield, R.G. Alberstein, L.M. Williamson, F.A. Tezcan. Determining the Structural and Energetic Basis of Allostery in a De Novo Designed Metalloprotein Assembly, J. Am. Chem. Soc. (2018).[PDF]


W.J. Song, J. Yu, F.A. Tezcan. Importance of scaffold flexibility/rigidity in the design and directed evolution of artificial metallo-β-lactamases, J. Am. Chem. Soc. (2017).[PDF]


L.A. Churchfield, F. Medina-Morales, J.D. Brodin, A. Perez, F.A. Tezcan. De Novo Design of an Allosteric Metalloprotein Assembly with Strained Disulfide Bonds, J. Am. Chem. Soc. (2016).[PDF]


S.J. Smith, R.J. Radford, R.H. Subramanian, B.R. Barnett, J.S. Figueroa, F.A. Tezcan. Tunable helicity, stability and DNA-binding properties of short peptides with hybrid metal coordination motifs, Chem. Sci. (2016).[PDF]


W.J. Song, F.A. Tezcan. A designed supramolecular protein assembly with in vivo enzymatic activity, Science 346, 1525-1528 (2014).[PDF]

Comments are closed