Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 59, Issue 42, Pages 18537-18545Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202008079
Keywords
C-13 detection; calcium binding; IDPs; side chains; water exchange
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Funding
- CERM/CIRMMP center of Instruct-ERIC
- Italian Ministry for University and Research (FOE funding)
- Fondazione CR Firenze
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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 alpha-synuclein, are then used to investigate how alpha-synuclein senses Ca(2+)concentration jumps associated with the transmission of nerve signals. Novel modules in the primary sequence of alpha-synuclein optimized for calcium sensing in highly flexible, disordered protein segments are identified.
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