earticle

영어

Green fluorescent protein (GFP) Nobel Prize protein from jellyfish is a versatile reporter protein for monitoring gene expression and protein localization in variety of systems. Applications using GFP reporters have expanded greatly due to the availability of mutants with altered spectral
prosperities, including several blue emission variants, all of which contains the single point mutation in tyrosine analogue in green fluorescent protein chromophore. Generally, GFP variants will be generated through replacement of naturally occurring amino acids by site directed mutation or directed evolution methodology and disadvantages of this methodology is limited with 20 naturally occurring side chains. In other hand unnatural amino acid mutagenesis has been used to selectively substitute target amino acids with our interesting side chains in our objective protein. Current studies have explored incorporation of unnatural amino acid analogues into green fluorescent protein and alter the spectral emission and excitation properties. We have selected different tyrosine analogues and successfully incorporated into GFP to alter the specific characters. We have selected the tyrosine analogues due to the important role in the chromophore and structure formation. Current study not only demonstrated the importance of unnatural amino acid mutagenesis and also demonstrated new approach to generate tailormade
proteins with interesting and useful spectral properties.