title: Intramolecular 1H-13C distance measurement in uniformly 13C, 15N labeled peptides by solid-state NMR.
abstract: A (1)H-(13)C frequency-selective REDOR (FS-REDOR) experiment is developed for measuring intramolecular (1)H-(13)C distances in uniformly (13)C, (15)N-labeled molecules. Theory and simulations show that the experiment removes the interfering homonuclear (1)H-(1)H, (13)C-(13)C and heteronuclear (1)H-(15)N, (13)C-(15)N dipolar interactions while retaining the desired heteronuclear (1)H-(13)C dipolar interaction. Our results indicate that this technique, combined with the numerical fitting, can be used to measure a (1)H-(13)C distance up to 5Å. We also demonstrate that the measured intramolecular (1)H-(13)C distances are useful to determine dihedral angles in proteins.
authors: Wuhan Institute of Physics and Mathematics, the Chinese Academy of Sciences, Wuhan 430071, China. lishenhui@wipm.ac.cn
authors: Shenhui
authors: S
authors: Li
authors: Yongchao
authors: Y
authors: Su
authors: Mei
authors: M
authors: Hong
mesh_terms: D006639:Histidine / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*
chemical_list: D010455:Peptides; D006639:Histidine; D009240:N-Formylmethionine Leucyl-Phenylalanine