Here, we review the contribution of protein engineering approaches, namely, the incorporation of unnatural amino acids and a biosynthetic CuA cofactor into the T1 copper protein azurin, to advancing the current understanding of how the unique structures of T1 copper and CuA centers confer their proteins with efficient and tailored ET properties.
Design of artificial proteins containing unnatural amino acids, backbone linkages or cofactors have also been reported, making it possible to prepare proteins with structural and functional properties beyond those of native proteins.
Finally, introducing unnatural amino acids or nonnative metal ions/prosthetic groups to expand the repertoires of metalloproteins have been demonstrated.
Incorporation of unnatural amino acids and non-native metal cofactors into proteins is an emerging field in the area of protein design, as it offers the tantalizing prospect of introducing new functionality and provides exquisite probes for and fine-tuning of native protein properties.
Although many of the sites have been modified with success, the relative paucity of functional group availability within proteinogenic amino acids can sometimes leave open questions about specific functions of the metal binding ligands.
Synthesis of;Pharmacological active peptide, Enzyme inhibitor, peptide nucleic acid, sugar peptide, fluorescently-labeled peptidecyclic pepide (disulfide and thioether linkage, depsipeptide), peptide mimetics, unnatural amino acid derivative, stable isotope labeled peptide (2H, 13C, 15N), antigen peptide (with epitope selection), and peptide conjugate for antibody production.
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Peptide libraries can be used to look for the sites of protein-protein or protein-nucleic acid interaction. Testing can be by direct capture of the protein or nucleic acid, by measurement of captured peptide, or by inhibition of another known binding interaction (Table 4). Protein sequences can be screened for interaction sites by making panels of antipeptide antibodies covering the whole protein (Table 5).