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Insight into the dynamic landscape of the multi-subunit protein, apoferritin, using neutron spectroscopy is presented in this paper. We combine elastic and quasi-elastic neutron scattering data, collected using different neutronspectrometers, to probe length scales up to 10 Å and timescales up to 2 ns. We show, for the first time without ambiguity, and via a thorough and systematic approach, that in its lyophilised form, apoferritin, above T ≈ 100 K and in the pico- to nanosecond time regime, exhibits a single dynamic response driven by methyl groupsalone. No contribution is observed from protons associated with non-methyl species. A distribution of CH3activation energies is obtained in line with the environmental heterogeneity that exists around the methyl species in this protein. In addition, by performing a complete and detailed analysis of the neutron scattering data, we prove the validity of the theoretical assumptions required by the methyl groupactivation model used to analyse the observed spectral response.
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