Electron paramagnetic resonance (EPR) spectroscopy provides a variety of tools to study
structures and structural changes of large biomolecules or complexes thereof. In order to …

The biological function of protein, DNA, and RNA molecules often depends on relative
movements of domains with dimensions of a few nanometers. This length scale can be …

PELDOR (or DEER; pulsed electron–electron double resonance) is an EPR (electron
paramagnetic resonance) method that measures via the dipolar electron–electron coupling …

Abstract Distances of 1.5 to 8 nm in macromolecules and supramolecular assemblies can be
measured by pulse electron paramagnetic resonance (EPR) experiments. In conjunction …

Applications of distance measurements by pulse dipolar electron-paramagnetic resonance
(PD-EPR) spectroscopy to structural biology are based on introducing spin labels (SLs) at …

Electron paramagnetic resonance (EPR) spectroscopy combined with site-directed spin
labelling is applicable to biomolecules and their complexes irrespective of system size and …

Macromolecular protein assemblies are of fundamental importance for many processes
inside the cell, as they perform complex functions and constitute central hubs where …

Pulse electron paramagnetic resonance measurements of long-range (nm scale) distances
between spin labels site-specifically attached to biomacromolecules have proven highly …

Recent developments in microwave technologies have led to a renaissance of electron
paramagnetic resonance (EPR) due to the implementation of new spectrometers operating …

The tertiary structure and conformational dynamics of ribonucleic acids (RNAs) are essential
for their function as biological catalysts, regulators, and structural scaffolds.[1] X-ray …