The study of how the intracellular medium influences protein structural dynamics and protein–
protein interactions is a captivating area of research for scientists aiming to comprehend …

Exploring the structure and dynamics of biomolecules in the context of their intracellular
environment has become the ultimate challenge for structural biology. As the cellular …

The development of ESR methods that measure long‐range distance distributions has
advanced biophysical research. However, the spin labels commonly employed are highly …

Site-directed spin labeling (SDSL) in combination with electron paramagnetic resonance
(EPR) spectroscopy allows studying the structure, dynamics, and interactions of proteins via …

The orchestrated interaction of transmembrane proteins with other molecules mediates
several crucial biological processes. Detergent solubilization may significantly alter or even …

Site-directed spin labeling using two strategically placed natural histidine residues allows for
the rigid attachment of paramagnetic Cu 2+. This double histidine (dHis) motif enables …

Instability of resin-dentin bonds is the Achilles' heel of adhesive dentistry. To address this
problem, a chelate-and-rinse extrafibrillar dentin demineralization strategy has been …

Abstract Distance determination by Electron Paramagnetic Resonance (EPR) based on
measurements of the dipolar coupling are technically challenging for electron spin systems …

Oligomerization of membrane proteins is common in nature. Here, we combine spin-labeling
double electron–electron resonance (DEER) and solid-state NMR (ssNMR) spectroscopy to …

Cu2+ based distance measurements using the double-histidine (dHis) motif by pulsed ESR
present an attractive strategy to obtain precise, narrow distance distributions that can be …