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

Different types of spin labels are currently available for structural studies of biomolecules
both in vitro and in cells using Electron Paramagnetic Resonance (EPR) and pulse dipolar …

The catalytic activity of human glutathione S‐transferase A1‐1 (hGSTA1‐1), a homodimeric
detoxification enzyme, is dependent on the conformational dynamics of a key C‐terminal …

The study of ever more complex biomolecular assemblies implicated in human health and
disease is facilitated by a suite of complementary biophysical methods. Pulse dipolar …

Pulsed dipolar EPR spectroscopy (PDS) in combination with site‐directed spin labeling is a
powerful tool in structural biology. However, the commonly used spin labels are conjugated …

In structural studies by NMR, pseudocontact shifts (PCSs) provide both angular and distance
information. For proteins, incorporation of a di-histidine (diHis) motif, coordinated to Co2+ …

Protein interaction studies often require very low concentrations and highly sensitive
biophysical methods. Here, we demonstrate that pulse dipolar electron paramagnetic …

Biomolecular applications of pulse dipolar electron paramagnetic resonance spectroscopy
(PDS) are becoming increasingly valuable in structural biology. Site-directed spin labelling …

Self-assembly of protein monomers directed by metal ion coordination constitutes a
promising strategy for designing supramolecular architectures complicated by the …

Recent advances in site-directed Cu2+ labeling of proteins and nucleic acids have added
an attractive new methodology to measure the structure-function relationship in …