Distance distribution information obtained by pulsed dipolar EPR spectroscopy provides an important contribution to many studies in structural biology. Increasingly, such information is used in integrative structural modeling, where it delivers unique restraints on the width of conformational ensembles. In order to ensure reliability of the structural models and of biological conclusions, we herein define quality standards for sample preparation and characterization, for measurements of distributed dipole–dipole couplings between paramagnetic labels, for conversion of the primary time-domain data into distance distributions, for interpreting these distributions, and for reporting results. These guidelines are substantiated by a multi-laboratory benchmark study and by analysis of data sets with known distance distribution ground truth. The study and the guidelines focus on proteins labeled with nitroxides and on double electron–electron resonance (DEER aka PELDOR) measurements and provide suggestions on how to proceed analogously in other cases.

Since the very first proposition of photonic crystals, their influence on the dynamics of spontaneous emission has been of great interest. The radiation dynamics is described by an integration kernel which\char22{}in a spectral representation\char22{}comprises two equally important contributions: the Lamb shift and the radiative contribution to the linewidth. The latter is connected to the density of states via Fermi's golden rule. To our knowledge, we present the first spatially resolved measurement of the complete radiation dynamics in a photonic crystal and of its local density of states over a wide spectral range. To this end we study a single magnetic dipole situated in a photonic crystal with a band gap at microwave frequencies and find non-Markovian behavior in excellent agreement with ab~initio calculations.

Site-directed spin labeling (SDSL) in combination with electron paramagnetic resonance (EPR) spectroscopy allows studying the structure, dynamics, and interactions of proteins via distance measurements in the nanometer range. We here give an overview of available spin labels, the strategies for their introduction into proteins, and the associated potentials for protein structural studies in vitro and in the context of living cells.

The chaperone Hsp90 remodels the structural ensemble of Tau, resulting in the formation of potentially neurotoxic oligomers.