Trapping Transient Protein Species by Genetic Code Expansion

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 noncanonical building blocks with tailored electronic and structural properties. 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 noncanonical 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.

Automated summary

Nature utilizes a limited number of genetically encoded amino acids to build functional proteins, but advancements in engineering the cellular translation machinery allow for the genetic encoding of noncanonical building blocks with tailored electronic and structural properties. Incorporating unique chemical functionality into proteins provides a powerful tool for exploring mechanisms and creating novel functions. Recent studies demonstrate how noncanonical amino acids have been used to capture and characterize reactive intermediates, adjust the catalytic properties of enzymes, and stabilize short-lived protein-protein complexes.