title: Determination of chemical shift anisotropies of unresolved carbonyl sites by C-alpha detection under magic-angle spinning.
abstract: We demonstrate that the static powder pattern line shape of chemical shift anisotropy (CSA) can be obtained for unresolved carbonyl sites of polypeptides under magic-angle spinning. The CSA interaction is first recoupled at the carbonyl site. The phase factors associated with the CSA recoupling are then transferred to the adjacent alpha carbon by an isotropic polarization transfer based on scalar spin-spin coupling. Because alpha carbons of polypeptides are usually better resolved, we can then obtain the CSA static powder pattern line shapes of the carbonyl sites after Fourier transformation in the second dimension. We validate our approach experimentally by measurements on [U-(13)C, (15)N]-l-alanine, [U-(13)C, (15)N]-l-valine and prion fibrils with uniform (13)C and (15)N labels on selected residues.
authors.affiliation: Department of Chemistry, National Taiwan University, No. 1 Section 4 Roosevelt Road, Taipei, Taiwan.
authors.forename: Yun
authors.initials: Y
authors.lastname: Mou
authors.forename: Peng-Huan
authors.initials: PH
authors.lastname: Chen
authors.forename: Hsin-Wen
authors.initials: HW
authors.lastname: Lee
authors.forename: Jerry C C
authors.initials: JC
authors.lastname: Chan
mesh_terms: D000409:Alanine / Q000737:chemistry*; D016880:Anisotropy; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011328:Prions / Q000737:chemistry*; D014633:Valine / Q000737:chemistry*
chemical_list: D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011328:Prions; D014633:Valine; D000409:Alanine