Scientific article

EPR Relaxation‐Enhancement‐Based Distance Measurements on Orthogonally Spin‐Labeled T4‐Lysozyme

Published inChemBioChem, vol. 14, no. 14, p. 1883-1890
Publication date2013-06-14
First online date2013-06-14

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.

  • EPR
  • Lanthanides
  • Nanometer-range distances
  • Nitroxide radicals
  • Proteins
Affiliation Not a UNIGE publication
Citation (ISO format)
RAZZAGHI, Sahand et al. EPR Relaxation‐Enhancement‐Based Distance Measurements on Orthogonally Spin‐Labeled T4‐Lysozyme. In: ChemBioChem, 2013, vol. 14, n° 14, p. 1883–1890. doi: 10.1002/cbic.201300165
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Article (Published version)
ISSN of the journal1439-4227

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