Measurement of the protein backbone dihedral angle phi based on quantification of remote CSA/DD interference in inter-residue 13C'(i - 1)-13Calpha(i) multiple-quantum coherences.
A novel triple-resonance NMR method is presented for the measurement of the protein backbone dihedral angle phi based on differential multiple-quantum relaxation induced by relaxation interference between 1Halpha(i)-13Calpha(i) dipolar and 13C'(i - 1) (carbonyl) chemical shift anisotropy mechanisms. The method employs a simultaneous transfer of 15N magnetization to the inter- and intra-residue 13Calpha carbons as well as the directly attached carbonyl carbon 13C'. Results obtained on 13C,15N-labeled ubiquitin demonstrate the potential of the method.
Kloiber
K
K
Institute of Organic Chemistry, University of Innsbruck, Austria.
Konrat
R
R
D016880:Anisotropy; D002247:Carbon Isotopes / Q000737:chemistry; D009587:Nitrogen Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011522:Protons; D013223:Statistics as Topic; D014452:Ubiquitins / Q000737:chemistry*
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011522:Protons; D014452:Ubiquitins