Earticle

초록

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

키워드

저자

• Niraikulam AYYADURAI [ School of Biotechnology, Yeungnam University, Gyeongsan, South Korea. ]
• Sun-Gu LEE [ Chemical Engineering, Busan National University ]
• Hyungdon YUN [ School of Biotechnology, Yeungnam University, Gyeongsan, South Korea. ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576