Measurement of homonuclear (2)J-couplings from spin-state selective double-/zero-quantum two-dimensional NMR spectra.
(1)H-detected two-dimensional double-/zero-quantum experiments are described for measurement of homonuclear (2)J(HH)-couplings of NH(2) or CH(2) groups in proteins. These experiments utilize multiple-quantum coherence for determination of the size and the absolute sign of the geminal scalar and dipolar couplings in the presence of broad lines. Spectra are simplified by gradient selection and spin-state selective filters.
Permi
P
P
Institute of Biotechnology, University of Helsinki, Helsinki, FIN-00014, Finland. Perttu.Permi@helsinki.fi
Heikkinen
S
S
Kilpeläinen
I
I
Annila
A
A
D002352:Carrier Proteins / Q000737:chemistry; D016207:Cytokines / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D009587:Nitrogen Isotopes; D011506:Proteins / Q000737:chemistry*; D014452:Ubiquitins / Q000737:chemistry
D002352:Carrier Proteins; D016207:Cytokines; D009587:Nitrogen Isotopes; D011506:Proteins; D014452:Ubiquitins; C066845:pleiotrophin