Correlation Engine 2.0
Clear Search sequence regions

  • electron (2)
  • help (1)
  • light (3)
  • LiPDS (3)
  • nucleic acids (1)
  • spin labels (3)
  • triplet (2)
  • Sizes of these terms reflect their relevance to your search.

    Measuring distances in biology at the molecular level is of great importance for understanding the structure and function of proteins, nucleic acids and other biological molecules and their complexes. Pulsed Dipolar Spectroscopy (PDS) offers advantages with respect to other methods as it is uniquely sensitive and specific to electronic spin centers and allows measurements in near-native conditions, comprising the in-cell environment. PDS methods measure the electron spin-spin dipolar interaction, therefore they require the presence of at least two paramagnetic centers, which are often stable radicals. Recent developments have introduced transient triplet states, photo-activated by a laser pulse, as spin labels and probes, thereby establishing a new family of techniques-Light-induced PDS (LiPDS). In this chapter, an overview of these methods is provided, looking at the chromophores that can be used for LiPDS and some of the technical aspects of the experiments. A guide to the choice of technique that can yield the best results, depending on the type of system studied and the information required, is provided. Examples of previous LiPDS studies of model systems and proteins are given. Characterization data for the chromophores used in these studies is tabulated to help selection of appropriate triplet state probes in future studies. Copyright © 2022 Elsevier Inc. All rights reserved.


    Arnau Bertran, Antonio Barbon, Alice M Bowen, Marilena Di Valentin. Light-induced pulsed dipolar EPR spectroscopy for distance and orientation analysis. Methods in enzymology. 2022;666:171-231

    Expand section icon Mesh Tags

    Expand section icon Substances

    PMID: 35465920

    View Full Text