Progresses of Single Molecular Fluorescence Resonance Energy Transfer in Studying Biomacromolecule Dynamic Process

Le Le SUN; Ying Ying SU; Yan Jing GAO; Wei Li; Hui LYU; Bin LI; Di LI

doi:10.1016/S1872-2040(18)61088-6

Progresses of Single Molecular Fluorescence Resonance Energy Transfer in Studying Biomacromolecule Dynamic Process

Le Le SUN
, Ying Ying SU
, Yan Jing GAO
, Wei Li
, Hui LYU
, Bin LI
, Di LI^*

^*Corresponding author for this work

Research output: Contribution to journal › Review article › peer-review

6 Scopus citations

Abstract

Biomacromolecules participate in various kinds of vital processes. Observing and analyzing their structural dynamic and the dynamic processes of intermolecular interaction at molecular level are important for understanding the action mechanism. Since its advent, single molecular fluorescence resonance energy transfer (SM-FRET) has demonstrated its great potential in studying conformational change and interaction process of biomacromolecules, and a series of new mechanisms have been revealed. This review summarized recent progresses of SM-FRET in studying protein structural dynamic, nucleic acid structural dynamic, protein-protein and protein-nucleic acid interactions.

Original language	English
Pages (from-to)	803-813
Number of pages	11
Journal	Chinese Journal of Analytical Chemistry
Volume	46
Issue number	6
DOIs	https://doi.org/10.1016/S1872-2040(18)61088-6
State	Published - Jun 2018
Externally published	Yes

Keywords

Biomacromolecule
Interaction
Review
Single molecular fluorescence resonance energy transfer
Structural dynamic

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10.1016/S1872-2040(18)61088-6

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@article{c8e7febe6f024294a1fb607fc9922cc3,

title = "Progresses of Single Molecular Fluorescence Resonance Energy Transfer in Studying Biomacromolecule Dynamic Process",

abstract = "Biomacromolecules participate in various kinds of vital processes. Observing and analyzing their structural dynamic and the dynamic processes of intermolecular interaction at molecular level are important for understanding the action mechanism. Since its advent, single molecular fluorescence resonance energy transfer (SM-FRET) has demonstrated its great potential in studying conformational change and interaction process of biomacromolecules, and a series of new mechanisms have been revealed. This review summarized recent progresses of SM-FRET in studying protein structural dynamic, nucleic acid structural dynamic, protein-protein and protein-nucleic acid interactions.",

keywords = "Biomacromolecule, Interaction, Review, Single molecular fluorescence resonance energy transfer, Structural dynamic",

author = "SUN, \{Le Le\} and SU, \{Ying Ying\} and GAO, \{Yan Jing\} and Wei Li and Hui LYU and Bin LI and Di LI",

note = "Publisher Copyright: {\textcopyright} 2018 Changchun Institute of Applied Chemistry, Chinese Academy of Sciences",

year = "2018",

month = jun,

doi = "10.1016/S1872-2040(18)61088-6",

language = "英语",

volume = "46",

pages = "803--813",

journal = "Chinese Journal of Analytical Chemistry",

issn = "0253-3820",

publisher = "Chinese Academy of Sciences",

number = "6",

}

TY - JOUR

T1 - Progresses of Single Molecular Fluorescence Resonance Energy Transfer in Studying Biomacromolecule Dynamic Process

AU - SUN, Le Le

AU - SU, Ying Ying

AU - GAO, Yan Jing

AU - Li, Wei

AU - LYU, Hui

AU - LI, Bin

AU - LI, Di

PY - 2018/6

Y1 - 2018/6

N2 - Biomacromolecules participate in various kinds of vital processes. Observing and analyzing their structural dynamic and the dynamic processes of intermolecular interaction at molecular level are important for understanding the action mechanism. Since its advent, single molecular fluorescence resonance energy transfer (SM-FRET) has demonstrated its great potential in studying conformational change and interaction process of biomacromolecules, and a series of new mechanisms have been revealed. This review summarized recent progresses of SM-FRET in studying protein structural dynamic, nucleic acid structural dynamic, protein-protein and protein-nucleic acid interactions.

AB - Biomacromolecules participate in various kinds of vital processes. Observing and analyzing their structural dynamic and the dynamic processes of intermolecular interaction at molecular level are important for understanding the action mechanism. Since its advent, single molecular fluorescence resonance energy transfer (SM-FRET) has demonstrated its great potential in studying conformational change and interaction process of biomacromolecules, and a series of new mechanisms have been revealed. This review summarized recent progresses of SM-FRET in studying protein structural dynamic, nucleic acid structural dynamic, protein-protein and protein-nucleic acid interactions.

KW - Biomacromolecule

KW - Interaction

KW - Review

KW - Single molecular fluorescence resonance energy transfer

KW - Structural dynamic

UR - https://www.scopus.com/pages/publications/85048627751

U2 - 10.1016/S1872-2040(18)61088-6

DO - 10.1016/S1872-2040(18)61088-6

M3 - 文献综述

AN - SCOPUS:85048627751

SN - 0253-3820

VL - 46

SP - 803

EP - 813

JO - Chinese Journal of Analytical Chemistry

JF - Chinese Journal of Analytical Chemistry

IS - 6

ER -

Progresses of Single Molecular Fluorescence Resonance Energy Transfer in Studying Biomacromolecule Dynamic Process

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Keywords

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