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- W3087086723 abstract "Abstract Many properties of intrinsically disordered proteins (IDPs), or protein regions (IDRs), are modulated by the nature of amino acid side chains as well as by local solvent exposure. We propose a set of exclusively heteronuclear NMR experiments to investigate these features in different experimental conditions that are relevant for physiological function. The proposed approach is generally applicable to many IDPs/IDRs whose assignment is available in the Biological Magnetic Resonance Bank (BMRB) to investigate how their properties are modulated by different, physiologically relevant conditions. The experiments, tested on α‐synuclein, are then used to investigate how α‐synuclein senses Ca 2+ concentration jumps associated with the transmission of nerve signals. Novel modules in the primary sequence of α‐synuclein optimized for calcium sensing in highly flexible, disordered protein segments are identified." @default.
- W3087086723 created "2020-09-25" @default.
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- W3087086723 date "2020-09-15" @default.
- W3087086723 modified "2023-09-26" @default.
- W3087086723 title "Monitoring the Interaction of α‐Synuclein with Calcium Ions through Exclusively Heteronuclear Nuclear Magnetic Resonance Experiments" @default.
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- W3087086723 doi "https://doi.org/10.1002/ange.202008079" @default.
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