Journal
JOURNAL OF BIOMOLECULAR NMR
Volume 53, Issue 4, Pages 293-301Publisher
SPRINGER
DOI: 10.1007/s10858-012-9639-0
Keywords
Intrinsically disordered proteins; C-13 detection; Non-uniform sampling; Multidimensional NMR experiment; Backbone assignment; Spin system identification
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Funding
- EC 7th Framework program BioNMR [261863]
- EC Marie Curie ITN program (IDPbyNMR) [264257]
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The characterization of intrinsically disordered proteins (IDPs) by NMR spectroscopy is made difficult by the extensive spectral overlaps. To overcome the intrinsic low-resolution of the spectra the introduction of high-dimensionality experiments is essential. We present here a set of high-resolution experiments based on direct C-13-detection which proved useful in the assignment of alpha-synuclein, a paradigmatic IDP. In particular, we describe the implementation of 4D HCBCACON, HCCCON, HCBCANCO, 4/5D HNCACON and HNCANCO and 3/4D HCANCACO experiments, specifically tailored for spin system identification and backbone resonances sequential assignment. The use of non-uniform-sampling in the indirect dimension and of the H-flip approach to achieve longitudinal relaxation enhancement rendered the experiments very practical.
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