Earticle

초록

영어

Single-molecule fluorescence resonance energy transfer (smFRET) analysis provides a variety of information including conformational and structural dynamics and localized or colocalized position of the tagged protein. For effective smFRET analysis of protein, site-specific dual-labeling with two fluorophores as an energy donor and an acceptor is crucial. We have shown that the site-specific labeling of protein via incorporation of an unnautural amino acid provides a greater contrast between the folded and unfolded states of the protein in smFRET analysis than the conventional labeling using double cysteines. As a model study, maltose-binding protein (MBP) was dually labeled via incorporation of ρ-azido-L-phenylalanine and cysteine at specific positions, immobilized on a surface, and subjected to smFRET analysis under native and denaturing conditions. The resulting histograms show that site-specific dual-labeling results in a more homogeneous distribution in protein populations. Considering this case of MBP, site-specific dual-labeling of the protein might offer a new chance for more precise smFRET analysis of the protein.

키워드

저자

• Moon-Hyeong SEO [ Dept. of Biological Sciences, KAIST, Daejeon 305-701. ]
• Tae-Sun LEE [ Dept. of Physics, KAIST, Daejeon 305-701. ]
• Eunkyung KIM [ Dept. of Biological Sciences, KAIST, Daejeon 305-701. ]
• Hee-Sung PARK [ Dept. of Chemistry, KAIST, Daejeon 305-701. ]
• Tae-Young YOON [ Dept. of Physics, KAIST, Daejeon 305-701. ]
• Hak-Sung KIM [ Dept. of Biological Sciences, KAIST, Daejeon 305-701. ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576