A new Gd3+ spin label for Gd3+-Gd3+ distance measurements in proteins produces narrow distance distributions

Elwy H Abdelkader, Michael D Lee, Akiva Feintuch, Marie Ramirez Cohen, James D Swarbrick, Gottfried Otting, Bim Graham, Daniella Goldfarb

Research output: Contribution to journalArticleResearchpeer-review

Abstract

Gd3+ tags have been shown to be useful for performing distance measurements in biomolecules via the double electron-electron resonance (DEER) technique at Q- and W-band frequencies. We introduce a new cyclen-based Gd3+ tag that exhibits a relatively narrow electron paramagnetic resonance (EPR) spectrum, affording high sensitivity, and which yields exceptionally narrow Gd3+-Gd3+ distance distributions in doubly tagged proteins owing to a very short tether. Both the maxima and widths of distance distributions measured for tagged mutants of the proteins ERp29 and T4 lysozyme, featuring Gd3+-Gd3+ distances of ca. 6 and 4 nm, respectively, were well reproduced by simulated distance distributions based on available crystal structures and sterically allowed rotamers of the tag. The precision of the position of the Gd3+ ion is comparable to that of the nitroxide radical in an MTSL-tagged protein and thus the new tag represents an attractive tool for performing accurate distance measurements and potentially probing protein conformational equilibria.
Original languageEnglish
Pages (from-to)5016-5021
Number of pages6
JournalJournal of Physical Chemistry Letters
Volume6
Issue number24
DOIs
Publication statusPublished - 2015

Keywords

  • double electron-electron resonance (DEER)
  • electron paramagnetic resonance

Cite this

Abdelkader, E. H., Lee, M. D., Feintuch, A., Cohen, M. R., Swarbrick, J. D., Otting, G., ... Goldfarb, D. (2015). A new Gd3+ spin label for Gd3+-Gd3+ distance measurements in proteins produces narrow distance distributions. Journal of Physical Chemistry Letters, 6(24), 5016-5021. https://doi.org/10.1021/acs.jpclett.5b02451
Abdelkader, Elwy H ; Lee, Michael D ; Feintuch, Akiva ; Cohen, Marie Ramirez ; Swarbrick, James D ; Otting, Gottfried ; Graham, Bim ; Goldfarb, Daniella. / A new Gd3+ spin label for Gd3+-Gd3+ distance measurements in proteins produces narrow distance distributions. In: Journal of Physical Chemistry Letters. 2015 ; Vol. 6, No. 24. pp. 5016-5021.
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abstract = "Gd3+ tags have been shown to be useful for performing distance measurements in biomolecules via the double electron-electron resonance (DEER) technique at Q- and W-band frequencies. We introduce a new cyclen-based Gd3+ tag that exhibits a relatively narrow electron paramagnetic resonance (EPR) spectrum, affording high sensitivity, and which yields exceptionally narrow Gd3+-Gd3+ distance distributions in doubly tagged proteins owing to a very short tether. Both the maxima and widths of distance distributions measured for tagged mutants of the proteins ERp29 and T4 lysozyme, featuring Gd3+-Gd3+ distances of ca. 6 and 4 nm, respectively, were well reproduced by simulated distance distributions based on available crystal structures and sterically allowed rotamers of the tag. The precision of the position of the Gd3+ ion is comparable to that of the nitroxide radical in an MTSL-tagged protein and thus the new tag represents an attractive tool for performing accurate distance measurements and potentially probing protein conformational equilibria.",
keywords = "double electron-electron resonance (DEER), electron paramagnetic resonance",
author = "Abdelkader, {Elwy H} and Lee, {Michael D} and Akiva Feintuch and Cohen, {Marie Ramirez} and Swarbrick, {James D} and Gottfried Otting and Bim Graham and Daniella Goldfarb",
year = "2015",
doi = "10.1021/acs.jpclett.5b02451",
language = "English",
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Abdelkader, EH, Lee, MD, Feintuch, A, Cohen, MR, Swarbrick, JD, Otting, G, Graham, B & Goldfarb, D 2015, 'A new Gd3+ spin label for Gd3+-Gd3+ distance measurements in proteins produces narrow distance distributions' Journal of Physical Chemistry Letters, vol. 6, no. 24, pp. 5016-5021. https://doi.org/10.1021/acs.jpclett.5b02451

A new Gd3+ spin label for Gd3+-Gd3+ distance measurements in proteins produces narrow distance distributions. / Abdelkader, Elwy H; Lee, Michael D; Feintuch, Akiva; Cohen, Marie Ramirez; Swarbrick, James D; Otting, Gottfried; Graham, Bim; Goldfarb, Daniella.

In: Journal of Physical Chemistry Letters, Vol. 6, No. 24, 2015, p. 5016-5021.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Abdelkader, Elwy H

AU - Lee, Michael D

AU - Feintuch, Akiva

AU - Cohen, Marie Ramirez

AU - Swarbrick, James D

AU - Otting, Gottfried

AU - Graham, Bim

AU - Goldfarb, Daniella

PY - 2015

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N2 - Gd3+ tags have been shown to be useful for performing distance measurements in biomolecules via the double electron-electron resonance (DEER) technique at Q- and W-band frequencies. We introduce a new cyclen-based Gd3+ tag that exhibits a relatively narrow electron paramagnetic resonance (EPR) spectrum, affording high sensitivity, and which yields exceptionally narrow Gd3+-Gd3+ distance distributions in doubly tagged proteins owing to a very short tether. Both the maxima and widths of distance distributions measured for tagged mutants of the proteins ERp29 and T4 lysozyme, featuring Gd3+-Gd3+ distances of ca. 6 and 4 nm, respectively, were well reproduced by simulated distance distributions based on available crystal structures and sterically allowed rotamers of the tag. The precision of the position of the Gd3+ ion is comparable to that of the nitroxide radical in an MTSL-tagged protein and thus the new tag represents an attractive tool for performing accurate distance measurements and potentially probing protein conformational equilibria.

AB - Gd3+ tags have been shown to be useful for performing distance measurements in biomolecules via the double electron-electron resonance (DEER) technique at Q- and W-band frequencies. We introduce a new cyclen-based Gd3+ tag that exhibits a relatively narrow electron paramagnetic resonance (EPR) spectrum, affording high sensitivity, and which yields exceptionally narrow Gd3+-Gd3+ distance distributions in doubly tagged proteins owing to a very short tether. Both the maxima and widths of distance distributions measured for tagged mutants of the proteins ERp29 and T4 lysozyme, featuring Gd3+-Gd3+ distances of ca. 6 and 4 nm, respectively, were well reproduced by simulated distance distributions based on available crystal structures and sterically allowed rotamers of the tag. The precision of the position of the Gd3+ ion is comparable to that of the nitroxide radical in an MTSL-tagged protein and thus the new tag represents an attractive tool for performing accurate distance measurements and potentially probing protein conformational equilibria.

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