title: Experiments and strategies for the assignment of fully 13C/15N-labelled polypeptides by solid state NMR.
abstract: 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.
authors.affiliation: Laboratorium für Physikalische Chemie, ETH Zentrum, Zürich, Switzerland.
authors.forename: S K
authors.initials: SK
authors.lastname: Straus
authors.forename: T
authors.initials: T
authors.lastname: Bremi
authors.forename: R R
authors.initials: RR
authors.lastname: Ernst
mesh_terms: 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*
chemical_list: D002247:Carbon Isotopes; D004151:Dipeptides; D009587:Nitrogen Isotopes; D010455:Peptides; D011506:Proteins; D014452:Ubiquitins