Abstract
Obtaining information on the structure and dynamics of intrinsically disordered proteins is challenging owing to the heterogeneous ensemble of rapidly interconverting structures which they populate. Consequently, any one technique gives only a particular view of the ensemble which may be biased to the chosen observable. Here, we use molecular simulations to bridge data from small-angle X-ray scattering, neutron spin-echo and single-molecule FRET experiments to obtain a unified picture of the dynamics of the disordered ensemble of prothymosin alpha.
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