Collection |

Nobel Prize in Chemistry 2018

The 2018 Nobel Prize in Chemistry was awarded to Frances H. Arnold “for the directed evolution of enzymes” and the other half jointly to George P. Smith and Gregory P. Winter “for the phage display of peptides and antibodies”. Together their pioneering work harnesses the processes of evolution for the generation of novel biological compounds. These tools have transformed the production of pharmaceuticals such as monoclonal antibodies and renewable fuels.

This Collection presents research, review, news and comment articles from Nature Research to celebrate the award. The collection content is editorially independent and the sole responsibility of Springer Nature.

The authors describe methods for the directed evolution of artificial endonuclease and ligase enzymes by X-SELEX, from diverse repertoires of synthetic genetic polymers (XNAzymes). The protocol has been applied to four different XNA chemistries and three different reactions, and it is, in principle, applicable to many more.

Protocol | | Nature Protocols

An artificial aldolase has been optimized using an ultrahigh-throughput microfluidic screening assay. The evolved enzyme exhibits excellent stereoselectivity and broad substrate scope. Structural studies suggest that a Lys-Tyr-Asn-Tyr catalytic tetrad, which emerged during directed evolution, is responsible for the >109 rate enhancement achieved by this catalyst.

Article | | Nature Chemistry

A computationally designed enzyme that was evolved to accelerate a chemical reaction 6 × 108-fold approaches the exceptional efficiency of highly optimized natural enzymes and provides valuable lessons for the creation of more sophisticated artificial catalysts.

Letter | | Nature

An artificial metalloenzyme is compartmentalized and evolved in vivo for olefin metathesis—an archetypal organometallic reaction without equivalent in nature; the evolved metathase reveals broad substrate scope and compares favourably with commercial catalysts.

Letter | | Nature

Allosteric effectors have the ability to modulate protein-ligand interactions in a controlled fashion. Now a novel class of antibody-like affinity reagents, synthetic antigen binders or sABs, are generated in vitro that target either the open or closed form of maltose-binding protein. These sABs can be engineered to control ligand-binding affinities by modulating the transition between different conformations.

Article | | Nature Structural & Molecular Biology

Metals serve as unique structural and functional elements in biology, providing a wealth of reactivities not available in a wholly proteinogenic active site. The computational redesign and directed evolution of zinc enzymes to create a phosphotriesterase provides insights into how these elements can be utilized in the development of new functions.

Article | | Nature Chemical Biology