Abstract
The temperature dependence of the Raman electron spin-lattice relaxation rate is a sensitive probe of the low-frequency vibrational spectrum of the structure surrounding a paramagnetic ion. If ρ(ν), the density of these low-frequency vibrational states, varies with frequency as a simple ν m−1 power law, then the Raman relaxation rate varies with temperature as T 3+2m at low temperatures, where m is the spectral dimension. In proteins m is found to be much reduced from the value of 3 that is normally observed in three-dimensional crystalline solids. Various theoretical models are discussed. Data are presented which contrast electron spin relaxation in proteins with that observed in amorphous materials (where two-level tunneling states are involved in the relaxation mechanism) and glasses (where the temporal profile of the spin recovery follows a stretched exponential).
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Stapleton, H.J. (1987). Spectral Dimensions of Paramagnetic Proteins. In: Barrett, T.W., Pohl, H.A. (eds) Energy Transfer Dynamics. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71867-0_20
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DOI: https://doi.org/10.1007/978-3-642-71867-0_20
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