A simple one-dimensional solid-state NMR method to characterize the nuclear spin interaction tensors associated with the peptide bond.
We propose a simple one-dimensional RF pulse sequence for the study of chemical shift and heteronuclear dipolar coupling tensors of oriented as well as unoriented solids. An off-resonance RF decoupling of protons during the signal acquisition of less sensitive nuclei is used to suppress homonuclear 1H-1H dipolar interactions. This method is experimentally demonstrated on peptide samples selectively labeled with 15N isotope.
Lee
D K
DK
Biophysics Research Division and Department of Chemistry, The University of Michigan, Ann Arbor, Michigan, 48109-1055, USA.
Ramamoorthy
A
A
D000465:Algorithms; D004578:Electron Spin Resonance Spectroscopy; D006859:Hydrogen / Q000737:chemistry; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008280:Magnetics; D009587:Nitrogen Isotopes; D010455:Peptides / Q000737:chemistry*; D011522:Protons; D011846:Radio Waves; D012815:Signal Processing, Computer-Assisted; D014633:Valine / Q000031:analogs & derivatives / Q000737:chemistry
D009587:Nitrogen Isotopes; D010455:Peptides; D011522:Protons; D006859:Hydrogen; D014633:Valine; C055589:N-acetylvaline