Electron paramagnetic resonance spectroscopy

John H. Golbeck, Art van der Est

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Scopus citations

Abstract

Electron paramagnetic resonance (EPR) spectroscopy is widely used to study proteins that contain naturally occurring paramagnetic centers and/or artificially introduced spin labels. In this chapter we present a mainly qualitative overview of the application of EPR spectroscopy to the study biological systems. The chapter begins with a short description of the physical principles underlying the method and the basic experimental techniques. An overview of characteristic lineshapes observed under various experimental conditions is then presented to show how quantities such as hyperfine couplings, g-anisotropy and zero-field splitting manifest themselves in EPR data. A number of specific examples are used to illustrate how these quantities can be used to obtain information about the geometry, bonding, electronic structure, etc. of biological systems.

Original languageEnglish (US)
Title of host publicationMolecular Biophysics for the Life Sciences
PublisherSpringer New York
Pages175-213
Number of pages39
ISBN (Electronic)9781461485483
ISBN (Print)9781461485476
DOIs
StatePublished - Jan 1 2013

All Science Journal Classification (ASJC) codes

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Social Sciences(all)

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    Golbeck, J. H., & van der Est, A. (2013). Electron paramagnetic resonance spectroscopy. In Molecular Biophysics for the Life Sciences (pp. 175-213). Springer New York. https://doi.org/10.1007/978-1-4614-8548-3_6