Protein structure and mechanism studied by electron nuclear double resonance spectroscopy

Victoria J. DeRose, Brian M. Hoffman

Research output: Contribution to journalArticlepeer-review

42 Scopus citations

Abstract

The information derived from measuring the electron-nuclear hyperfine interaction can be used for analysis of both structure and mechanism in biomolecules, provided an EPR signal exists. The examples given here illustrate the usefulness of the multiple techniques now available for the Electron nuclear double resonance (ENDOR) measurement, as well as the importance of isotopic labeling within the biological system under study. ENDOR spectroscopy recovers this information by measuring the nuclear magnetic resonance (NMR) spectra of nuclei associated with the electron spin, as detected by changes in the EPR spectrum of that spin. This chapter provides a more detailed description of the hyperfine interaction as measured by ENDOR spectroscopy, a description of ENDOR instrumentation, and the types of ENDOR experiments that can be performed. Finally, examples of the application of ENDOR spectroscopy to a variety of biomolecules are described.

Original languageEnglish (US)
Pages (from-to)554-589
Number of pages36
JournalMethods in enzymology
Volume246
Issue numberC
DOIs
StatePublished - Jan 1 1995

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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