A new method has been developed that makes it possible to site-specifically incorporate unnatural amino acids into proteins. Synthetic amino acids were incorporated into the enzyme beta-lactamase by the use of a chemically acylated suppressor transfer RNA that inserted the amino acid in response to a stop codon substituted for the codon encoding residue of interest. Peptide mapping localized the inserted amino acid to a single peptide, and enough enzyme could be generated for purification to homogeneity. The catalytic properties of several mutants at the conserved Phe66 were characterized. The ability to selectively replace amino acids in a protein with a wide variety of structural and electronic variants should provide a more detailed understanding of protein structure and function.

https://science.sciencemag.org/content/sci/244/4901/182.full.pdf

A general method for site-specific incorporation of unnatural amino acids into proteins.

https://zenodo.org/record/1259717/files/article.pdf

Advances in the Synthesis of Oligonucleotides by the Phosphoramidite Approach

Simultaneous multiple peptide synthesis under continuous flow conditions on cellulose paper discs as segmental solid supports

The p-nitrophenylethyl (NPE) group: A versatile new blocking group for phosphate and aglycone protection in nucleosides and nucleotides

It is fifty years since the first chemical synthesis of a dinucleoside phosphate and a dinucleotide with natural 3′→5′-internucleotide linkages was reported The main developments in the methodology of oligo- and poly-nucleotide synthesis that have taken place since are described

M. Ubasawa

Papers

Synthesis of the 3'-terminal decaribonucleoside nonaphosphate of yeast alanine transfer ribonucleic acid