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 neutron spectrometers, 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 groups alone. No contribution is observed from protons associated with non-methyl species. A distribution of CH₃ activation 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 group activation model used to analyse the observed spectral response.