Studying DNA-protein interactions with single-molecule Forster resonance energy transfer

被引：10
作者：
Farooq, Shazia [1 ]
Fijen, Carel [1 ]
Hohlbein, Johannes [1 ]
机构：
[1] Wageningen UR, Biophys Lab, Wageningen, Netherlands
来源：
PROTOPLASMA | 2014年 / 251卷 / 02期
关键词：
Single-molecule Forster resonance energy transfer; Fluorescence; Enzymes; DNA; DNA-protein interactions; RNA-POLYMERASE-II; PROBABILITY-DISTRIBUTION ANALYSIS; MULTIPARAMETER FLUORESCENCE DETECTION; ALTERNATING-LASER EXCITATION; NANO-POSITIONING SYSTEM; ATOMIC-FORCE MICROSCOPE; 3.3 ANGSTROM RESOLUTION; COLI REP HELICASE; ESCHERICHIA-COLI; STRUCTURAL BASIS;
D O I：
10.1007/s00709-013-0596-6
中图分类号：
Q94 [植物学];
学科分类号：
071001 ;
摘要：
Single-molecule Forster resonance energy transfer (smFRET) has emerged as a powerful tool for elucidating biological structure and mechanisms on the molecular level. Here, we focus on applications of smFRET to study interactions between DNA and enzymes such as DNA and RNA polymerases. SmFRET, used as a nanoscopic ruler, allows for the detection and precise characterisation of dynamic and rarely occurring events, which are otherwise averaged out in ensemble-based experiments. In this review, we will highlight some recent developments that provide new means of studying complex biological systems either by combining smFRET with force-based techniques or by using data obtained from smFRET experiments as constrains for computer-aided modelling.
引用
收藏
页码：317 / 332
页数：16
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