EPR distance measurements in deuterated proteins

Hassane El Mkami, David G. Norman (Lead / Corresponding author)

    Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)peer-review

    31 Citations (Scopus)

    Abstract

    Pulsed electron double resonance technique, also known as double electron-electron resonance, jointly with site-directed spin labeling (SDSL) have been used extensively for studying structures and structural change. During the last decades, significant enhancements have been made by optimization of the experimental protocols, introducing new techniques for artifact suppression, and developing data analysis programs for extracting more reliable distance distributions. However, the distance determination by pulsed electron paramagnetic resonance is still facing some limitations, especially when studying spin-labeled proteins, due mainly to the fast relaxation time that imposes severe limitations on the maximum distances measurable and upon the sensitivity of such experiments. In the present work, we demonstrate the impact of the deuteration of the underlying protein, in addition to the solvent, on relaxation times, sensitivity, and on distance measurements.

    Original languageEnglish
    Title of host publicationElectron paramagnetic resonance investigations of biological systems by using spin labels, spin probes, and intrinsic metal ions, Part B
    EditorsPeter Z. Qin, Kurt Warncke
    PublisherAcademic Press
    Pages125-152
    Number of pages28
    ISBN (Print)9780128028353
    DOIs
    Publication statusPublished - 2015

    Publication series

    NameMethods in enzymology
    PublisherAcademic Press
    Volume564
    ISSN (Print)0076-6879

    Keywords

    • Algorithms
    • Animals
    • Deuterium
    • Electron spin resonance Spectroscopy
    • Humans
    • Proteins
    • Spin labels
    • Journal article

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