Single Pair Förster Resonance Energy Transfer: A Versatile Tool To Investigate Protein Conformational Dynamics

BioEssays ◽  
2018 ◽  
Vol 40 (3) ◽  
pp. 1700078 ◽  
Author(s):  
Lena Voith von Voithenberg ◽  
Don C. Lamb
Keyword(s):  
Energy Transfer ◽  
Conformational Dynamics ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Forster Resonance Energy Transfer ◽  
Förster Resonance Energy Transfer ◽  
Single Pair ◽  
Protein Conformational Dynamics ◽  
Versatile Tool ◽  
Förster Resonance

EXPLORING THE FOLDING FREE ENERGY LANDSCAPE OF SMALL RNA MOLECULES BY SINGLE-PAIR FÖRSTER RESONANCE ENERGY TRANSFER

2008 ◽  
Vol 03 (04) ◽  
pp. 439-457 ◽  
Author(s):  
ANDREI YU. KOBITSKI ◽  
ALEXANDER NIERTH ◽  
MARTIN HENGESBACH ◽  
ANDRES JÄSCHKE ◽  
MARK HELM ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Small Rnas ◽  
Energy Landscape ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Forster Resonance Energy Transfer ◽  
Förster Resonance Energy Transfer ◽  
Single Pair ◽  
Rna Molecules ◽  
Förster Resonance

Proteins and RNA are biological macromolecules built from linear polymers. The process by which they fold into compact, well-defined, three-dimensional architectures to perform their functional tasks is still not well understood. It can be visualized by Brownian motion of an ensemble of molecules through a rugged energy landscape in search of an energy minimum corresponding to the native state. To explore the conformational energy landscape of small RNAs, single pair Förster resonance energy transfer (spFRET) experiments on solutions as well as on surface-immobilized samples have provided new insights. In this review, we focus on our recent work on two FRET-labeled small RNAs, the Diels-Alderase (DAse) ribozyme and the human mitochondrial tRNA Lys . For both RNAs, three different conformational states can be distinguished, and the associated mean FRET efficiencies provide clues about their structural properties. The systematic variation of their free energies with the concentration of Mg 2+ counterions was analyzed quantitatively by using a thermodynamic model that separates conformational changes from Mg 2+ binding. Furthermore, time-resolved spFRET studies on immobilized DAse reveal slow interconversions between intermediate and folded states on the time scale of ~ 100 ms. The quantitative data obtained from spFRET experiments may likely assist in the further development of theories and models addressing the folding dynamics and (counterion-dependent) energetics of RNA molecules.

scholarly journals Combining MFD and PIE for Accurate Single-Pair Förster Resonance Energy Transfer Measurements

ChemPhysChem ◽  
2012 ◽  
Vol 13 (4) ◽  
pp. 1060-1078 ◽  
Author(s):  
Volodymyr Kudryavtsev ◽  
Martin Sikor ◽  
Stanislav Kalinin ◽  
Dejana Mokranjac ◽  
Claus A. M. Seidel ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Forster Resonance Energy Transfer ◽  
Förster Resonance Energy Transfer ◽  
Single Pair ◽  
Förster Resonance
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