Abstract
We report an investigation of the magnetic core of the biomolecule ferritin by means of proton nuclear magnetic resonance (NMR) and relaxation, magnetic susceptibility and scanning electron microscope (SEM) measurements. SEM images show that the outer protein shell is taken out completely by an appropriate chemical treatment and indicate particle sizes ranging from 102 to 104 nm. Susceptibility measurements show a maximum in the zero-field-cooled data which is strongly field-dependent and can be ascribed to superparamagnetic behavior, whereas the hysteresis curve is different from normal ferritin. Proton NMR and spin-lattice relaxation data as a function of temperature at 4.7 T suggest the presence of an antiferromagnetic transition around 100 K.
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Jang, Z.H., Suh, B.J., Lascialfari, A. et al. Proton NMR and susceptibility measurements on the magnetic core of ferritin. Appl. Magn. Reson. 19, 557–562 (2000). https://doi.org/10.1007/BF03162400
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DOI: https://doi.org/10.1007/BF03162400