Ensemble and single-molecule FRET studies of protein synthesis.
Ensemble and single-molecule FRET studies of protein synthesis.
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DOI：
10.1016/j.ymeth.2017.12.007
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发表时间：
2018-03-15
期刊：
影响因子：
--
通讯作者：
Ermolenko DN
中科院分区：
文献类型：
--
作者：
Lai WC;Ermolenko DN
Protein synthesis is a complex, multi-step process that involves large conformational changes of the ribosome and protein factors of translation. Over the last decade, Förster resonance energy transfer (FRET) has become instrumental for studying structural rearrangements of the translational apparatus. Here, we discuss the design of ensemble and single-molecule (sm) FRET assays of translation. We describe a number of experimental strategies that can be used to introduce fluorophores into the ribosome, tRNA, mRNA and protein factors of translation. Alternative approaches to tethering of translation components to the microscope slide in smFRET experiments are also reviewed. Finally, we discuss possible challenges in the interpretation of FRET data and ways to address these challenges.
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