Pulsed dipolar electron paramagnetic resonance spectroscopy (PDS) is a valuable method
for determining biomolecular structures and their conformational changes during function …

The established model-free methods for the processing of two-electron dipolar spectroscopy
data [DEER (double electron-electron resonance), PELDOR (pulsed electron double …

Metal ions are important for the folding, structure, and function of biomolecules. Thus,
knowing where their binding sites are located in proteins or oligonucleotides is a critical …

Quantum information processing promises to revolutionise computing; quantum algorithms
have been discovered that address common tasks significantly more efficiently than their …

Combining rigid Cu (II) labels and pulsed-EPR techniques enables distance constraint
measurements that are incisive probes of protein structure and dynamics. However, the …

A homoleptic bisnitroxide complex of manganese (II) was synthesized as a model system for
EPR spectroscopic distance determinations involving high-spin metal ions and more than …

Distance measurements in biological macromolecules represent a very active field of
application of pulsed electron paramagnetic resonance (EPR) spectroscopy. The relatively …

We explore the potential of orientation-resolved pulsed dipolar spectroscopy (PDS) in light-
induced versions of the experiment. The use of triplets as spin-active moieties for PDS offers …

Pulsed electron–electron double resonance (PELDOR or DEER) spectroscopy is frequently
used to determine distances between spin centres in biomacromolecular systems …

We present a new photoswitchable spin label for light-induced pulsed electron
paramagnetic resonance dipolar spectroscopy (LiPDS), the photoexcited triplet state of …