
AbstractCarbon‐13 direct‐detection NMR methods have proved to be very useful for the characterization of intrinsically disordered proteins (IDPs). Here we present a suite of experiments in which amino‐acid‐selective editing blocks are encoded in CACON‐ and CANCO‐type sequences to give 13C‐detected spectra containing correlations arising from a particular type or group of amino acid(s). These two general types of experiments provide the complementary intra‐ and inter‐residue correlations necessary for sequence‐specific assignment of backbone resonance frequencies. We demonstrate the capabilities of these experiments on two IDPs: fully reduced Cox17 and WIPC. The proposed approach constitutes an independent strategy to simplify crowded spectra as well as to perform sequence‐specific assignment, thereby demonstrating its potential to study IDPs.
Carbon Isotopes, Magnetic Resonance Spectroscopy, Proteins, IDP, NMR, heteronuclear NMR; intrinsically disordered proteins; NMR spectroscopy; protein structure, Amino Acids
Carbon Isotopes, Magnetic Resonance Spectroscopy, Proteins, IDP, NMR, heteronuclear NMR; intrinsically disordered proteins; NMR spectroscopy; protein structure, Amino Acids
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