TY - JOUR
T1 - Application of fluorescence resonance energy transfer in protein studies
AU - Ma, Linlin
AU - Yang, Fan
AU - Zheng, Jie
PY - 2014/12/5
Y1 - 2014/12/5
N2 - Since the physical process of fluorescence resonance energy transfer (FRET) was elucidated more than six decades ago, this peculiar fluorescence phenomenon has turned into a powerful tool for biomedical research due to its compatibility in scale with biological molecules as well as rapid developments in novel fluorophores and optical detection techniques. A wide variety of FRET approaches have been devised, each with its own advantages and drawbacks. Especially in the last decade or so, we are witnessing a flourish of FRET applications in biological investigations, many of which exemplify clever experimental design and rigorous analysis. Here we review the current stage of FRET methods development with the main focus on its applications in protein studies in biological systems, by summarizing the basic components of FRET techniques, most established quantification methods, as well as potential pitfalls, illustrated by example applications.
AB - Since the physical process of fluorescence resonance energy transfer (FRET) was elucidated more than six decades ago, this peculiar fluorescence phenomenon has turned into a powerful tool for biomedical research due to its compatibility in scale with biological molecules as well as rapid developments in novel fluorophores and optical detection techniques. A wide variety of FRET approaches have been devised, each with its own advantages and drawbacks. Especially in the last decade or so, we are witnessing a flourish of FRET applications in biological investigations, many of which exemplify clever experimental design and rigorous analysis. Here we review the current stage of FRET methods development with the main focus on its applications in protein studies in biological systems, by summarizing the basic components of FRET techniques, most established quantification methods, as well as potential pitfalls, illustrated by example applications.
KW - Assembly
KW - Fluorophore
KW - FRET
KW - Microscopy
KW - Protein
KW - Spectroscopy
UR - http://www.scopus.com/inward/record.url?scp=84907666160&partnerID=8YFLogxK
U2 - 10.1016/j.molstruc.2013.12.071
DO - 10.1016/j.molstruc.2013.12.071
M3 - Article
VL - 1077
SP - 87
EP - 100
JO - Journal of Molecular Structure
JF - Journal of Molecular Structure
SN - 0022-2860
ER -