Journal
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY C-PHOTOCHEMISTRY REVIEWS
Volume 12, Issue 1, Pages 20-30Publisher
ELSEVIER
DOI: 10.1016/j.jphotochemrev.2011.05.001
Keywords
Fluorescence resonance energy transfer; FRET methods; Quantum dots; Fluorophore labeling; Protein folding
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Funding
- German Research Foundation (DFG) [SFB 67]
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Forster resonance energy transfer (FRET) in association with the recent advancements in optical techniques provides a way to understand the detailed mechanisms in different biological systems at the molecular level. Improvements in wide-field, confocal and two-photon microscopy facilitate the measurements of two-dimensional spatial distribution in steady-state as well as dynamic bimolecular interactions. In the recent decade, FRET became an exceptional Fluorescence-based technique due to its potential advantages for studying the biological processes in living cells and more for spatial resolution at nanometer scale. In particular, FRET investigations have shown that biomolecules adopt different conformational structures to perform their functions. In this review, the basic principles and applications of FRET in chemistry, biology, and physics are discussed. Along with, the recent improvements in fluorophore design and labeling and FRET measurement methods are briefly mentioned. (C) 2011 Elsevier B.V. All rights reserved.
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