5D 13C-detected experiments for backbone assignment of unstructured proteins with a very low signal dispersion
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Bacillus subtilis enzymology MeSH
- Bacterial Proteins chemistry MeSH
- DNA-Directed RNA Polymerases chemistry MeSH
- Carbon Isotopes MeSH
- Protein Conformation MeSH
- Nuclear Magnetic Resonance, Biomolecular methods MeSH
- Proteins chemistry MeSH
- Amino Acid Sequence MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Bacterial Proteins MeSH
- DNA-Directed RNA Polymerases MeSH
- Carbon Isotopes MeSH
- Proteins MeSH
Two novel 5D NMR experiments (CACONCACO, NCOCANCO) for backbone assignment of disordered proteins are presented. The pulse sequences exploit relaxation properties of the unstructured proteins and combine the advantages of (13)C-direct detection, non-uniform sampling, and longitudinal relaxation optimization to maximize the achievable resolution and minimize the experimental time. The pulse sequences were successfully tested on the sample of partially disordered delta subunit from RNA polymerase from Bacillus subtilis. The unstructured part of this 20 kDa protein consists of 81 amino acids with frequent sequential repeats. A collection of 0.0003% of the data needed for a conventional experiment with linear sampling was sufficient to perform an unambiguous assignment of the disordered part of the protein from a single 5D spectrum.
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