MAPPING GLOBAL FOLDS OF OLIGONUCLEOTIDES BY PULSED ELECTRON-ELECTRON DOUBLE RESONANCE

Olav Schiemann

Research output: Contribution to journalReview articlepeer-review

24 Citations (Scopus)

Abstract

The understanding of structure-dynamics-function relationships in oligonucleotides or oligonucleotide/protein complexes calls for biophysical methods that can resolve the structure and dynamics of such systems on the critical nanometer length scale. A modern electron paramagnetic resonance (EPR) method called pulsed electron-electron double resonance (PELDOR or DEER) has been shown to reliably and precisely provide distances and distance distributions in the range of 1.5-8 nm. In addition, recent experiments proved that a PELDOR experiment also contains information on the orientation of labels, enables easy separation of coupling mechanisms and allows for counting the number of monomers in complexes. This chapter briefly summarizes the theory, describes how to perform and analyze such experiments and discusses the limitations.

Original languageEnglish
Pages (from-to)329-351
Number of pages23
JournalMethods In Enzymology
Volume469
DOIs
Publication statusPublished - 2009

Keywords

  • METAL-ION BINDING
  • HAMMERHEAD RIBOZYME
  • PARAMAGNETIC-RESONANCE
  • EPR SPECTROSCOPY
  • CONFORMATIONAL FLEXIBILITY
  • DISTANCE MEASUREMENTS
  • PELDOR MEASUREMENTS
  • HIGH-AFFINITY
  • SPIN-ECHO
  • SITE

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