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- W3158082151 abstract "Nuclear magnetic resonance (NMR) has long been instrumental in the characterization of intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs). This method continues to offer rich insights into the nature of IDPs in solution, especially in combination with other biophysical methods such as small-angle scattering, single-molecule fluorescence, electron paramagnetic resonance (EPR), and mass spectrometry. Substantial advances have been made in recent years in studies of proteins containing both ordered and disordered domains and in the characterization of problematic sequences containing repeated tracts of a single or a few amino acids. These sequences are relevant to disease states such as Alzheimer's, Parkinson's, and Huntington's diseases, where disordered proteins misfold into harmful amyloid. Innovative applications of NMR are providing novel insights into mechanisms of protein aggregation and the complexity of IDP interactions with their targets. As a basis for understanding the solution structural ensembles, dynamic behavior, and functional mechanisms of IDPs and IDRs, NMR continues to prove invaluable." @default.
- W3158082151 created "2021-05-10" @default.
- W3158082151 creator A5060626982 @default.
- W3158082151 creator A5061288516 @default.
- W3158082151 date "2021-10-01" @default.
- W3158082151 modified "2023-10-15" @default.
- W3158082151 title "NMR illuminates intrinsic disorder" @default.
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- W3158082151 doi "https://doi.org/10.1016/j.sbi.2021.03.015" @default.
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