title: Sensitivity-enhanced static 15N NMR of solids by 1h indirect detection.
abstract: A method for enhancing the sensitivity of 15N spectra of nonspinning solids through 1H indirect detection is introduced. By sampling the 1H signals in the windows of a pulsed spin-lock sequence, high-sensitivity 1H spectra can be obtained in two-dimensional (2D) spectra whose indirect dimension yields the 15N chemical shift pattern. By sacrificing the 1H chemical shift information, sensitivity gains of 1.8 to 2.5 for the 15N spectra were achieved experimentally. A similar sensitivity enhancement was also obtained for 2D (15)N-(1)H dipolar and 15N chemical shift correlation spectroscopy, by means of a 3D 1H/15N-1H/15N correlation experiment. We demonstrate this technique, termed PRINS for proton indirectly detected nitrogen static NMR, on a crystalline model compound with long 1H T(1rho) and on a 25-kDa protein with short 1H T(1rho). This 1H indirect detection approach should be useful for enhancing the sensitivity of 15N NMR of oriented membrane peptides. It can also be used to facilitate the empirical optimization of 15N-detected experiments where the inherent sensitivity of the sample is low.
authors.affiliation: Department of Chemistry, Iowa State University, Ames, Iowa 50011, USA.
authors.forename: M
authors.initials: M
authors.lastname: Hong
authors.forename: S
authors.initials: S
authors.lastname: Yamaguchi
mesh_terms: D003087:Colicins / Q000737:chemistry*; D005998:Glycine / Q000031:analogs & derivatives; D007473:Ion Channels / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011208:Powders; D017434:Protein Structure, Tertiary; D012680:Sensitivity and Specificity
chemical_list: D003087:Colicins; D007473:Ion Channels; D008565:Membrane Proteins; D009587:Nitrogen Isotopes; D011208:Powders; D005998:Glycine