Abstract
IN iminoxyl free radicals1 there is an odd electron localized usually at the nitrogen–oxygen bond. Because of the tensor anisotropy of dipole–dipole interactions and g-tensor anisotropy, the electron spin resonance spectrum of these radicals is quite sensitive to changes in the mobility of free radicals. The correlation time, τ, which can be found by width analysis of certain components of the electron spin resonance spectrum, is a characteristic of the tumbling motion rate of the free radicals2,3. Using iminoxyl free radicals, with various substituents, reacting specifically with certain functional groups of proteins, it is possible to obtain free radicals labelled with macromolecules4,5.
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GRIGORIAN, G., KALMANSON, A., ROZANTZEV, E. et al. Electron Spin Resonance Investigation of Conformation Changes in Serum Albumin with the Help of Iminoxyl Paramagnetic Label. Nature 216, 927–928 (1967). https://doi.org/10.1038/216927a0
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DOI: https://doi.org/10.1038/216927a0
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