title: BSH-CP based 3D solid-state NMR experiments for protein resonance assignment.
abstract: We have recently presented band-selective homonuclear cross-polarization (BSH-CP) as an efficient method for CO-CA transfer in deuterated as well as protonated solid proteins. Here we show how the BSH-CP CO-CA transfer block can be incorporated in a set of three-dimensional (3D) solid-state NMR (ssNMR) pulse schemes tailored for resonance assignment of proteins at high static magnetic fields and moderate magic-angle spinning rates. Due to the achieved excellent transfer efficiency of 33 % for BSH-CP, a complete set of 3D spectra needed for unambiguous resonance assignment could be rapidly recorded within 1 week for the model protein ubiquitin. Thus we expect that BSH-CP could replace the typically used CO-CA transfer schemes in well-established 3D ssNMR approaches for resonance assignment of solid biomolecules.
authors.affiliation: Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.
authors.forename: Chaowei
authors.initials: C
authors.lastname: Shi
authors.forename: Hannes K
authors.initials: HK
authors.lastname: Fasshuber
authors.forename: Veniamin
authors.initials: V
authors.lastname: Chevelkov
authors.forename: Shengqi
authors.initials: S
authors.lastname: Xiang
authors.forename: Birgit
authors.initials: B
authors.lastname: Habenstein
authors.forename: Suresh Kumar
authors.initials: SK
authors.lastname: Vasa
authors.forename: Stefan
authors.initials: S
authors.lastname: Becker
authors.forename: Adam
authors.initials: A
authors.lastname: Lange
mesh_terms: D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D011506:Proteins / Q000737:chemistry*; D025801:Ubiquitin / Q000737:chemistry
chemical_list: D011506:Proteins; D025801:Ubiquitin