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Trapping transient protein species by genetic code expansion.

Research paper by Matthias M Tinzl, Donald D Hilvert

Indexed on: 19 Aug '20Published on: 19 Aug '20Published in: ChemBioChem



Abstract

Nature employs a limited number of genetically encoded amino acids for the construction of functional proteins. By engineering components of the cellular translation machinery, however, it is now possible to genetically encode non-canonical building blocks with tailored electronic and structural properties, enabling facile chemical diversification of these biopolymers. The ability to incorporate unique chemical functionality into proteins provides a powerful tool to probe mechanism and create novel function. In this minireview, we highlight several recent studies that illustrate how non-canonical amino acids have been used to capture and characterize reactive intermediates, fine-tune the catalytic properties of enzymes, and stabilize short-lived protein-protein complexes. © 2020 Wiley-VCH GmbH.