Chemical modification of proteins with bioorthogonal reaction and site-selectivity has been increasingly
recognized for exquisite control over homogeneity and geometry, allowing more complex and various applications
of proteins. The development of novel bioorthogonal reactions and their adaptation to protein chemistry in the form
of genetically encoded non-natural amino acids are fueling widespread use of the so-called ‘bioorthogonal protein
conjugation’. Site-specific incorporation of a non-natural amino acid technique precisely delivers a bioorthogonal
group to any defined site in response to an expanded genetic code where a selective bond-forming reaction equips
proteins with novel functionalities in a chemically well-defined and homogeneous manner.
Keywords: Non-natural amino acid, bioorthogonal reaction, site-specific incorporation, bioconjugation, protein evolution, genetic code.
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