Earticle

초록

영어

Green Fluorescent Protein (GFP) is an indispensable tool with a wide range of application as reporter protein in the cellular and biological studies. It helps in direct visualization of bimolecular and biochemical activities of the living cells. Although a wide range of GFP variant has been generated, developing a far red fluorescent protein in an indispensable quest in the cell biology for the purpose of deep tissue and whole cell imaging. For this purpose, enormous effort has been done by the researchers to generate far red fluorescent proteins through incorporation of natural and unnatural amino acid in the chromophore of GFP. In this study, we have generated a highly red shifted GFP by incorporating the tyrosine analog, amino tyrosine which provides the GFP with the inherent characteristics of Red fluorescent protein (RFP) such as emission maximum at longer wavelength and copper sensing characteristics. This study offers an insight into the spectral properties of amino tyrosine incorporated GFP and the mechanism of fluorescence quenching in response to copper concentration. The Copper binding property of the engineered protein was characterized by the combination of fluorescent spectroscopy, absorption spectroscopy and circular dichroism. Overall this study demonstrates that the development of red shifted GFP with inherent characteristics of red fluorescent protein.

키워드

저자

• Saravananprabhu NADARAJAN [ School of Biotechnology,Yeungnam University, Gyeongsan, Korea. ]
• Hyungdon YUN [ School of Biotechnology,Yeungnam University, Gyeongsan, Korea. ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576