Single-Molecular Forster Resonance Energy Transfer Measurement on Structures and Interactions of Biomolecules

被引：22

作者：

Qiao, Yi ^{[1
]}

Luo, Yuhan ^{[1
]}

Long, Naiyun ^{[1
]}

Xing, Yi ^{[2
]}

Tu, Jing ^{[1
]}

机构：

[1] Southeast Univ, Sch Biol Sci & Med Engn, State Key Lab Bioelect, Nanjing 210096, Peoples R China

[2] Peking Univ, Sch Publ Hlth, Inst Child & Adolescent Hlth, Beijing 100191, Peoples R China

来源：

MICROMACHINES | 2021年 / 12卷 / 05期

基金：

中国国家自然科学基金;

关键词：

FRET; smFRET; biomolecule; nucleic acid structure; protein; INDUCED CONFORMATIONAL-CHANGES; SIGNAL-TRANSDUCTION; INTRINSIC DISORDER; LIVING CELLS; G-QUADRUPLEX; TRANSMEMBRANE HELICES; HOLLIDAY JUNCTIONS; FRET SIGNATURES; FLUORESCENCE; DYNAMICS;

D O I：

10.3390/mi12050492

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

Single-molecule Forster resonance energy transfer (smFRET) inherits the strategy of measurement from the effective "spectroscopic ruler" FRET and can be utilized to observe molecular behaviors with relatively high throughput at nanometer scale. The simplicity in principle and configuration of smFRET make it easy to apply and couple with other technologies to comprehensively understand single-molecule dynamics in various application scenarios. Despite its widespread application, smFRET is continuously developing and novel studies based on the advanced platforms have been done. Here, we summarize some representative examples of smFRET research of recent years to exhibit the versatility and note typical strategies to further improve the performance of smFRET measurement on different biomolecules.

引用

页数：22

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[41] Forster resonance energy transfer-based cholesterolysis assay identifies a novel hedgehog inhibitor [J].

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[49] Single Pair Forster Resonance Energy Transfer: A Versatile Tool To Investigate Protein Conformational Dynamics [J].

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