title: Sequential backbone assignment based on dipolar amide-to-amide correlation experiments.
abstract: Proton detection in solid-state NMR has seen a tremendous increase in popularity in the last years. New experimental techniques allow to exploit protons as an additional source of information on structure, dynamics, and protein interactions with their surroundings. In addition, sensitivity is mostly improved and ambiguity in assignment experiments reduced. We show here that, in the solid state, sequential amide-to-amide correlations turn out to be an excellent, complementary way to exploit amide shifts for unambiguous backbone assignment. For a general assessment, we compare amide-to-amide experiments with the more common (13)C-shift-based methods. Exploiting efficient CP magnetization transfers rather than less efficient INEPT periods, our results suggest that the approach is very feasible for solid-state NMR.
authors.affiliation: Department for NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
authors.forename: ShengQi
authors.initials: S
authors.lastname: Xiang
authors.forename: Kristof
authors.initials: K
authors.lastname: Grohe
authors.forename: Petra
authors.initials: P
authors.lastname: Rovó
authors.forename: Suresh Kumar
authors.initials: SK
authors.lastname: Vasa
authors.forename: Karin
authors.initials: K
authors.lastname: Giller
authors.forename: Stefan
authors.initials: S
authors.lastname: Becker
authors.forename: Rasmus
authors.initials: R
authors.lastname: Linser
mesh_terms: D000577:Amides / Q000737:chemistry*; D000818:Animals; D002645:Chickens; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D013049:Spectrin / Q000737:chemistry
chemical_list: D000577:Amides; D011506:Proteins; D013049:Spectrin