Journal
CHEMBIOCHEM
Volume 13, Issue 16, Pages 2425-2432Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201200447
Keywords
intrinsically disordered proteins; NMR spectroscopy; protein structure
Funding
- Joint Research Activity and Access to Research Infrastructures (BioNMR, EC) [261863]
- Marie Curie ITN program (IDP-byNMR, EC) in the EC 7th framework program [264257]
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Carbon-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 C-13-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.
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