Analysis and simulation of these time traces can reveal the relative distance and, for rigid systems, orientation distributions of the two moieties, (6−10) providing information about the structure and conformation of the (bio)molecule(s) to which these moieties are attached. (1−5) The dipolar interaction between two moieties with nonzero electronic spin is measured as an oscillating time trace. Alternatively, the summed spectrum enables an orientation-independent analysis to determine the distance distribution.Įlectron spin resonance (ESR) pulsed dipolar spectroscopy (PDS) is an invaluable biophysical technique for studying complex biological assemblies. For the first time, we measure a 2D frequency-correlated laser-induced magnetic dipolar spectrum, and we are able to monitor the complete orientation dependence of the system in a single experiment. We exploit the complementary information provided by the different light-induced techniques to yield atomic-level structural information. ![]() Herein we present a comprehensive analysis of the orientation selection of a full set of light-induced PDS experiments. The rigidity leads to orientation selection effects in PDS, which can be analyzed to give both distance and mutual orientation information. Cofactors are often rigidly bound within the protein structure, providing an accurate positional marker. ![]() The use of triplets as spin-active moieties for PDS offers an attractive tool for studying biochemical systems containing optically active cofactors. We explore the potential of orientation-resolved pulsed dipolar spectroscopy (PDS) in light-induced versions of the experiment.
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