Abstract
The spectroscopy of electron paramagnetic resonance, unlike optical methods, allows observing paramagnetic molecules inside a non-paramagnetic matrix of any morphology, which makes it possible to investigate the behavior of proteins immobilized on porous carriers. In the present work the preferential orientation of lysozyme from chicken egg white, spin-labeled in position his-15, immobilized on the surface of a series of porous oxide carriers, has been defined by computer simulation of the dynamic EPR spectra.
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