Structural Information from CW-EPR Spectra of Dipolar Coupled Nitroxide Spin Labels

  • Eric J. Hustedt
  • Albert H. Beth
Part of the Biological Magnetic Resonance book series (BIMR, volume 19)


Site directed spin labeling has emerged as a powerful technique for determining structural features of proteins. By incorporating two spin labeled side chains, distances between elements of secondary structure can be determined by quantitation of spin-spin interactions between the probes. Recent advances in methods for extracting both the distance between spin labeled probes and their relative orientations are providing the capability for testing and refining accurate structural models for a wide variety of proteins. These methods take advantage of multifrequency EPR and global non-linear data analysis tools. The capabilities of current analytical methods are described for three relevant models of spin-spin interactions and directions for further refinement of these methods for future applications are described. Reliable structural information can be obtained for interelectron distances ranging from 5 to 20 Å and up to 25 Å using perdeuterated probes.


Electron Paramagnetic Resonance Spin Label Dipolar Coupling Rotational Correlation Time Interspin Distance 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Kluwer Academic / Plenum Publishers, New York 2002

Authors and Affiliations

  • Eric J. Hustedt
    • 1
  • Albert H. Beth
    • 1
  1. 1.Department of Molecular Physiology and BiophysicsVanderbilt UniversityNashvilleUSA

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