title: Dipolar dynamic frequency shifts in multiple-quantum spectra of methyl groups in proteins: correlation with side-chain motion.
abstract: Small deviations from the expected relative positions of multiplet components in double- and zero-quantum 1H-13C methyl correlation maps have been observed in spectra recorded on a 7-kDa protein. These dynamic frequency shifts (DFS) are the result of dipolar cross-correlations that derive from fields produced by the spins within the methyl groups. The shifts have been quantified and compared with values calculated from a Redfield analysis. Good agreement is noted between the signs of the predicted and experimentally observed relative shifts of lines in both F1 and F2 dimensions of spectra, as well as between the magnitudes of the calculated and observed shifts in the F2 (1H) dimension. The experimental DFS values show a reasonable correlation with 2H relaxation-derived measures of methyl side-chain dynamics, as expected from theory. This suggests that in cases where such shifts can be quantified, they can serve as qualitative measures of motion.
authors.affiliation: Department of Medical Genetics, University of Toronto, Toronto, Ontario, M5S 1A8, Canada.
authors.forename: Vitali
authors.initials: V
authors.lastname: Tugarinov
authors.forename: Jason E
authors.initials: JE
authors.lastname: Ollerenshaw
authors.forename: Lewis E
authors.initials: LE
authors.lastname: Kay
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D002247:Carbon Isotopes; D007553:Isotope Labeling; D008745:Methylation; D008956:Models, Chemical; D019906:Nuclear Magnetic Resonance, Biomolecular; D011506:Proteins / Q000737:chemistry*; D011522:Protons; D011789:Quantum Theory
chemical_list: D000596:Amino Acids; D002247:Carbon Isotopes; D011506:Proteins; D011522:Protons