Abstract
Intrinsically disordered proteins (IDPs) play a prominent role in normal cell physiology and pathological conditions. However, experimental characterization of complex conformational equilibria in IDPs remain a major challenge. Hydrodynamic radius Rh is a measurable parameter which reports on compactness of an IDP chain. We used the double stimulated echo NMR pulse sequence to obtain Rh data for several disordered proteins in a range of urea concentration from 0 to 10 M. Dioxan molecule was used as an internal standard to account for changes in solvent viscosity.
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