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Owing to its absolute sensitivity and to its selectivity to paramagnetic species, site\u2010directed spin labeling (SDSL) combined with electron paramagnetic resonance (EPR) has the potential to evolve into an efficient method to follow conformational changes in proteins directly inside cells. Until now, the use of nitroxide\u2010based spin labels for in\u2010cell studies has represented a major hurdle because of their short persistence in the cellular context. The design and synthesis of the first maleimido\u2010proxyl\u2010based spin label (M\u2010TETPO) resistant towards reduction and being efficient to probe protein dynamics by continuous wave and pulsed EPR is presented. 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