Experiments and strategies for the assignment of fully 13C/15N-labelled polypeptides by solid state NMR.
High-resolution heteronuclear NMR correlation experiments and strategies are proposed for the assignment of fully 13C/15N-labelled polypeptides in the solid state. By the combination of intra-residue and inter-residue 13C-15N correlation experiments with 13C-13C spin-diffusion studies, it becomes feasible to partially assign backbone and side-chain resonance in solid proteins. The performance of sequences using 15N instead of 13C detection is evaluated regarding sensitivity and resolution for a labelled dipeptide (L-Val-L-Phe). The techniques are used for a partial assignment of the 15N and 13C resonances in human ubiquitin.
Straus
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SK
Laboratorium für Physikalische Chemie, ETH Zentrum, Zürich, Switzerland.
Bremi
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T
Ernst
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RR
D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D004151:Dipeptides / Q000737:chemistry; D006801:Humans; D008956:Models, Chemical; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012680:Sensitivity and Specificity; D014452:Ubiquitins / Q000737:chemistry*
D002247:Carbon Isotopes; D004151:Dipeptides; D009587:Nitrogen Isotopes; D010455:Peptides; D011506:Proteins; D014452:Ubiquitins