FRET (fluorescence resonance energy transfer) sheds light on transcription

2011 ◽  
Vol 39 (1) ◽  
pp. 122-127 ◽  
Author(s):  
Dina Grohmann ◽  
Daniel Klose ◽  
Daniel Fielden ◽  
Finn Werner
Keyword(s):  
Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Structural Rearrangement ◽  
Atomic Level ◽  
Dynamic Nature ◽  
X Ray ◽  
Fluorescence Techniques ◽  
Complex Organization ◽  
Transcription Complexes

The complex organization of the transcription machinery has been revealed mainly by biochemical and crystallographic studies. X-ray structures describe RNA polymerases and transcription complexes on an atomic level, but fail to portray their dynamic nature. The use of fluorescence techniques has made it possible to add a new layer of information to our understanding of transcription by providing details about the structural rearrangement of mobile elements and the network of interactions within transcription complexes in solution and in real-time.

scholarly journals Comment on “Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water”

Science ◽  
2018 ◽  
Vol 361 (6405) ◽  
pp. eaar7101 ◽  
Author(s):  
Robert B. Best ◽  
Wenwei Zheng ◽  
Alessandro Borgia ◽  
Karin Buholzer ◽  
Madeleine B. Borgia ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Small Angle ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Disordered Proteins ◽  
Förster Resonance Energy Transfer ◽  
Unfolded Proteins ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

Riback et al. (Reports, 13 October 2017, p. 238) used small-angle x-ray scattering (SAXS) experiments to infer a degree of compaction for unfolded proteins in water versus chemical denaturant that is highly consistent with the results from Förster resonance energy transfer (FRET) experiments. There is thus no “contradiction” between the two methods, nor evidence to support their claim that commonly used FRET fluorophores cause protein compaction.

Enhanced X-ray Excited Luminescence of LaF3:Ce/CdSeS Nanocomposites by Resonance Energy Transfer for Radiation Detection

2017 ◽  
Vol 46 (8) ◽  
pp. 5319-5323 ◽  
Author(s):  
Jinsik Ju ◽  
Hayeon Won ◽  
JinJoo Jung ◽  
Junyeob Yeo ◽  
Phan Van Cuong ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Radiation Detection ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
X Ray ◽  
Excited Luminescence

Quantum Dot Bioconjugates as Energy Donors in Fluorescence Resonance Energy Transfer Assays

2003 ◽  
Vol 773 ◽  
Author(s):  
Aaron R. Clapp ◽  
Igor L. Medintz ◽  
J. Matthew Mauro ◽  
Hedi Mattoussi
Keyword(s):  
Energy Transfer ◽  
Quantum Dot ◽  
Organic Dyes ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Genetically Engineered ◽  
Molar Ratio ◽  
Binding Assays ◽  
Specific Sequence ◽  
Donor Acceptor

AbstractLuminescent CdSe-ZnS core-shell quantum dot (QD) bioconjugates were used as energy donors in fluorescent resonance energy transfer (FRET) binding assays. The QDs were coated with saturating amounts of genetically engineered maltose binding protein (MBP) using a noncovalent immobilization process, and Cy3 organic dyes covalently attached at a specific sequence to MBP were used as energy acceptor molecules. Energy transfer efficiency was measured as a function of the MBP-Cy3/QD molar ratio for two different donor fluorescence emissions (different QD core sizes). Apparent donor-acceptor distances were determined from these FRET studies, and the measured distances are consistent with QD-protein conjugate dimensions previously determined from structural studies.

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