Measuring Nanometer Distances in Proteins and Rigid Rulers between <sup>19</sup>F and Gd<sup>3+</sup> by Integration of <sup>19</sup>F-ENDOR Signal Intensities

<sup>19</sup>F ENDOR is emerging as a powerful tool in structural biology for measuring distances in proteins labeled with <sup>19</sup>F and a paramagnetic tag. Due to spin-spin relaxation and line width limitations, it has been difficult to determine intertag distances larger than about 15 Å. Using a set of geometrically well-defined rulers and spin-labeled proteins, we show that <sup>19</sup>F-Gd<sup>3+</sup> distances up to 20 Å can be accessed by integrating the intensity of the ENDOR spectrum, with distances approaching 30 Å potentially in reach as well. This method is robust when the intensities are scaled to a known reference, and provides scope for nanometer-scale triangulation of the coordinates of a ligand in a protein-ligand complex.

Authors

Institutions

Publication Details

Journal
Journal of the American Chemical Society
Published
2025-05-06
DOI
https://doi.org/10.1021/jacs.4c13530
Citations
4
Primary Topic
Electron Spin Resonance Studies
Type
article
Field-Weighted Citation Impact
6.54

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Measuring Nanometer Distances in Proteins and Rigid Rulers between 19F and Gd3+ by Integration of 19F-ENDOR Signal Intensities

Adelheid Godt, Gottfried Otting, Nicholas J. Cox, Anton Savitsky et al.
4 citations
Journal of the American Chemical Society
Electron Spin Resonance Studies
6.54
article

Measuring Nanometer Distances in Proteins and Rigid Rulers between 19F and Gd3+ by Integration of 19F-ENDOR Signal Intensities

Adelheid Godt, Gottfried Otting, Nicholas J. Cox, Anton Savitsky, Haocheng Qianzhu, Elwy H. Abdelkader, Martyna Judd, Mian Qi, Thomas Huber, Jeffrey R. Harmer
article en
4 citations

Abstract

<sup>19</sup>F ENDOR is emerging as a powerful tool in structural biology for measuring distances in proteins labeled with <sup>19</sup>F and a paramagnetic tag. Due to spin-spin relaxation and line width limitations, it has been difficult to determine intertag distances larger than about 15 Å. Using a set of geometrically well-defined rulers and spin-labeled proteins, we show that <sup>19</sup>F-Gd<sup>3+</sup> distances up to 20 Å can be accessed by integrating the intensity of the ENDOR spectrum, with distances approaching 30 Å potentially in reach as well. This method is robust when the intensities are scaled to a known reference, and provides scope for nanometer-scale triangulation of the coordinates of a ligand in a protein-ligand complex.

Journal of the American Chemical SocietyVol. 147(20)
Australian National University (AU), The University of Queensland (AU), TU Dortmund University (DE), Bielefeld University (DE), ARC Centre of Excellence for Innovations in Peptide and Protein Science (AU), ARC Centre of Excellence in Advanced Molecular Imaging (AU)
Westpac Scholars Trust, Australian Research Council
Openalex Percentile: Top 4%
Electron Spin Resonance Studies
6.54
DOISourceOpenAlex
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.