AI Article Synopsis
- Genetic code expansion (GCE) has transformed protein chemistry by allowing the incorporation of over 150 noncanonical amino acids (ncAAs) into proteins across different organisms.
- The incorporation of ncAAs typically occurs within an open reading frame, where the requirement for peptide bond formation at the α-amine limits the variety of molecules that can be genetically encoded.
- By including the initiator position in GCE, researchers can insert a wider range of diverse molecules, some of which may not have an α-amine, highlighting various methods for initiating protein synthesis both in vitro and in vivo.
Article Abstract
Genetic code expansion (GCE) has revolutionized the field of protein chemistry. Over the past several decades more than 150 different noncanonical amino acids (ncAAs) have been co-translationally installed into proteins within various host organisms. The vast majority of these ncAAs have been incorporated between the start and stop codons within an open reading frame. This requires that the ncAA be able to form a peptide bond at the α-amine, limiting the types of molecules that can be genetically encoded. In contrast, the α-amine of the initiating amino acid is not required for peptide bond formation. Therefore, including the initiator position in GCE allows for co-translational insertion of more diverse molecules that are modified, or completely lacking an α-amine. This review explores various methods which have been used to initiate protein synthesis with diverse molecules both in vitro and in vivo.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7237318 | PMC |
| http://dx.doi.org/10.1002/cbic.202000017 | DOI Listing |
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