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- W2015367561 endingPage "3045" @default.
- W2015367561 startingPage "3034" @default.
- W2015367561 abstract "The realization that a protein can be fully functional even in the absence of a stable three-dimensional structure has motivated a large number of studies describing the conformational behaviour of these proteins at atomic resolution. Here, we review recent advances in the determination of local structural propensities of intrinsically disordered proteins (IDPs) from experimental NMR chemical shifts. A mapping of the local structure in IDPs is of paramount importance in order to understand the molecular details of complex formation, in particular, for IDPs that fold upon binding or undergo structural transitions to pathological forms of the same protein. We discuss experimental strategies for the spectral assignment of IDPs, chemical shift prediction algorithms and the generation of representative structural ensembles of IDPs on the basis of chemical shifts. Additionally, we highlight the inherent degeneracies associated with the determination of IDP sub-state populations from NMR chemical shifts alone." @default.
- W2015367561 created "2016-06-24" @default.
- W2015367561 creator A5001250430 @default.
- W2015367561 creator A5018221555 @default.
- W2015367561 creator A5044113826 @default.
- W2015367561 creator A5080147321 @default.
- W2015367561 date "2013-06-21" @default.
- W2015367561 modified "2023-09-24" @default.
- W2015367561 title "Conformational Propensities of Intrinsically Disordered Proteins from NMR Chemical Shifts" @default.
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