ArticleChembiochem : a European journal of chemical biology2013
EPR relaxation-enhancement-based distance measurements on orthogonally spin-labeled T4-lysozyme.
Article in Chembiochem : a European journal of chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 19 citations in OpenAlex.
- RIDME Spectroscopy: New Topics Beyond the Determination of Electron Spin-Spin Distances.The journal of physical chemistry letters · 2025Review
- Triarylmethyl Radicals: EPR Study ofZeitschrift fur physikalische Chemie (Frankfurt am Main, Germany) · 2017Article
- Room-Temperature Electron Spin Relaxation of Triarylmethyl Radicals at the X- and Q-Bands.The journal of physical chemistry. B · 2015Article
- Long-range distance measurements in proteins at physiological temperatures using saturation recovery EPR spectroscopy.Journal of the American Chemical Society · 2014Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Lanthanide-induced enhancement of the longitudinal relaxation of nitroxide radicals in combination with orthogonal site-directed spin labeling is presented as a systematic distance measurement method intended for studies of bio-macromolecules and bio-macromolecular complexes. The approach is tested on a water-soluble protein (T4-lysozyme) for two different commercially available lanthanide labels, and complemented by previously reported data on a membrane-inserted polypeptide. Single temperature measurements are shown to be sufficient for reliable distance determination, with an upper measurable distance limit of about 5-6 nm. The extracted averaged distances represent the closest approach in Ln(III) -nitroxide distance distributions. Studies of conformational changes and of bio-macromolecule association-dissociation are proposed as possible application area of the relaxation-enhancement-based distance measurements.
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