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• W4253291274 endingPage "13710" @default.
• W4253291274 startingPage "13707" @default.
• W4253291274 abstract "Abstract Characterization of the conformational ensemble of disordered proteins is highly important for understanding protein folding and aggregation mechanisms, but remains a computational and experimental challenge owing to the dynamic nature of these proteins. New observables that can provide unique insights into transient residual structures in disordered proteins are needed. Here using denatured ubiquitin as a model system, NMR solvent paramagnetic relaxation enhancement (sPRE) measurements provide an accurate and highly sensitive probe for detecting low populations of residual structure in a disordered protein. Furthermore, a new ensemble calculation approach based on sPRE restraints in conjunction with residual dipolar couplings (RDCs) and small‐angle X‐ray scattering (SAXS) is used to define the conformational ensemble of disordered proteins at atomic resolution. The approach presented should be applicable to a wide range of dynamic macromolecules." @default.
• W4253291274 created "2022-05-12" @default.
• W4253291274 creator A5008234020 @default.
• W4253291274 creator A5050207878 @default.
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• W4253291274 date "2018-09-12" @default.
• W4253291274 modified "2023-10-18" @default.
• W4253291274 title "Conformational Ensemble of Disordered Proteins Probed by Solvent Paramagnetic Relaxation Enhancement (sPRE)" @default.
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• W4253291274 doi "https://doi.org/10.1002/ange.201807365" @default.
• W4253291274 hasPublicationYear "2018" @default.
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