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)

    21 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

    Fingerprint

    Electrons
    Proteins
    Electron Spin Resonance Spectroscopy
    Artifacts

    Keywords

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

    Cite this

    El Mkami, H., & Norman, D. G. (2015). EPR distance measurements in deuterated proteins. In P. Z. Qin, & K. Warncke (Eds.), Electron paramagnetic resonance investigations of biological systems by using spin labels, spin probes, and intrinsic metal ions, Part B (pp. 125-152). (Methods in enzymology; Vol. 564). Academic Press. https://doi.org/10.1016/bs.mie.2015.05.027
    El Mkami, Hassane ; Norman, David G. / EPR distance measurements in deuterated proteins. Electron paramagnetic resonance investigations of biological systems by using spin labels, spin probes, and intrinsic metal ions, Part B. editor / Peter Z. Qin ; Kurt Warncke. Academic Press, 2015. pp. 125-152 (Methods in enzymology).
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    El Mkami, H & Norman, DG 2015, EPR distance measurements in deuterated proteins. in PZ Qin & K Warncke (eds), Electron paramagnetic resonance investigations of biological systems by using spin labels, spin probes, and intrinsic metal ions, Part B. Methods in enzymology, vol. 564, Academic Press, pp. 125-152. https://doi.org/10.1016/bs.mie.2015.05.027

    EPR distance measurements in deuterated proteins. / El Mkami, Hassane; Norman, David G. (Lead / Corresponding author).

    Electron paramagnetic resonance investigations of biological systems by using spin labels, spin probes, and intrinsic metal ions, Part B. ed. / Peter Z. Qin; Kurt Warncke. Academic Press, 2015. p. 125-152 (Methods in enzymology; Vol. 564).

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

    TY - CHAP

    T1 - EPR distance measurements in deuterated proteins

    AU - El Mkami, Hassane

    AU - Norman, David G.

    N1 - © 2015 Elsevier Inc. All rights reserved.

    PY - 2015

    Y1 - 2015

    N2 - 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.

    AB - 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.

    KW - Algorithms

    KW - Animals

    KW - Deuterium

    KW - Electron spin resonance Spectroscopy

    KW - Humans

    KW - Proteins

    KW - Spin labels

    KW - Journal article

    U2 - 10.1016/bs.mie.2015.05.027

    DO - 10.1016/bs.mie.2015.05.027

    M3 - Chapter (peer-reviewed)

    C2 - 26477250

    SN - 9780128028353

    T3 - Methods in enzymology

    SP - 125

    EP - 152

    BT - Electron paramagnetic resonance investigations of biological systems by using spin labels, spin probes, and intrinsic metal ions, Part B

    A2 - Qin, Peter Z.

    A2 - Warncke, Kurt

    PB - Academic Press

    ER -

    El Mkami H, Norman DG. EPR distance measurements in deuterated proteins. In Qin PZ, Warncke K, editors, Electron paramagnetic resonance investigations of biological systems by using spin labels, spin probes, and intrinsic metal ions, Part B. Academic Press. 2015. p. 125-152. (Methods in enzymology). https://doi.org/10.1016/bs.mie.2015.05.027