Spectroscopically Orthogonal Labelling to Disentangle Site-Specific Nitroxide Label Distributions.

ABSTRACT: Biomolecular applications of pulse dipolar electron paramagnetic resonance spectroscopy (PDS) are becoming increasingly valuable in structural biology. Site-directed spin labelling of proteins is routinely performed using nitroxides, with paramagnetic metal ions and other organic radicals gaining popularity as alternative spin centres. Spectroscopically orthogonal spin labelling using different types of labels potentially increases the information content available from a single sample. When analysing experimental distance distributions between two nitroxide spin labels, the site-specific rotamer information has been projected into the distance and is not readily available, and the contributions of individual labelling sites to the width of the distance distribution are not obvious from th

SUBMITTER: Vitali V 

PROVIDER: S-EPMC10861635 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature