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Monitoring the Interaction of α‐Synuclein with Calcium Ions through Exclusively Heteronuclear Nuclear Magnetic Resonance Experiments
Author(s) -
Pontoriero Letizia,
Schiavina Marco,
Murrali Maria Grazia,
Pierattelli Roberta,
Felli Isabella C.
Publication year - 2020
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.202008079
Subject(s) - heteronuclear molecule , chemistry , intrinsically disordered proteins , calcium , biophysics , chemical physics , nuclear magnetic resonance , nuclear magnetic resonance spectroscopy , biochemistry , physics , stereochemistry , biology , organic chemistry
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.