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Issue 15, 2011
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Thermal motion in the multi-subunit protein, apoferritin, as probed by high energy resolution neutron spectroscopy

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Abstract

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.

Graphical abstract: Thermal motion in the multi-subunit protein, apoferritin, as probed by high energy resolution neutron spectroscopy

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Publication details

The article was received on 06 Apr 2011, accepted on 31 May 2011 and first published on 24 Jun 2011


Article type: Paper
DOI: 10.1039/C1SM05603D
Citation: Soft Matter, 2011,7, 6934-6941
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    Thermal motion in the multi-subunit protein, apoferritin, as probed by high energy resolution neutron spectroscopy

    Mark. T. F. Telling , C. Neylon, L. Clifton, S. Howells, L. van Eijck and V. G. Sakai, Soft Matter, 2011, 7, 6934
    DOI: 10.1039/C1SM05603D

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