About the Seminar

Design and evolution of artificial metalloenzymes

Enzyme design represents a formidable challenge. We do not fully understand the rules of protein folding, and our knowledge of structure-function relationships in these macromolecules is at best incomplete. Nature has solved the problem of protein design through the mechanism of Darwinian evolution. From primitive peptidic precursors, recursive cycles of mutation, selection and amplification of molecules with favorable traits have given rise to all of the many thousands of gene products in every one of our cells. An analogous process of natural selection can be profitably exploited in silico and in the laboratory on a human time scale to create, characterize and optimize artificial catalysts for tasks unimagined by Nature. Recent progress in combining computational and evolutionary approaches for the design of artificial metalloenzymes will be discussed, together with insights into enzyme function gained from studies of the engineered catalysts.

About the Speaker 

Donald Hilvert obtained his Ph.D. in Chemistry in 1983 from Columbia University.  Following postdoctoral work at Rockefeller University, he started his academic career on the faculty of the Scripps Research Institute in La Jolla, California.  Since October 1997, he has been Professor in the Laboratory of Organic Chemistry at the ETH Zurich (Zurich, Switzerland).  Professor Hilvert’s research program utilizes the tools of chemical biology to study and engineer proteins, including designer enzymes and molecular containers. These efforts have been recognized by a number of awards, including the Pfizer Award in Enzyme Chemistry, the Protein Society Emil Thomas Kaiser Award, and the Ronald Breslow Award for Achievement in Biomimetic Chemistry. He is an elected member of the American Academy of Arts and Sciences and received an honorary doctorate from Uppsala University.

Host: Noah Burns