화학공학소재연구정보센터
Journal of the American Chemical Society, Vol.119, No.39, 9274-9278, 1997
Sensitivity enhancement of triple-resonance protein NMR spectra by proton evolution of multiple-quantum coherences using a simultaneous H-1 and C-13 constant-time evolution period
Short transverse relaxation times of C-alpha and H-alpha single-quantum states in proteins reduce signal-to-noise ratios of heteronuclear correlation experiments involving transfers of C-alpha and H-alpha coherences. To overcome this ''short transverse relaxation problem'', we have developed a simultaneous H-1 and C-13 constant-time (sim-CT) heteronuclear multiple-quantum coherence (HMQC) scheme. New features in this design include: (i) utilization of heteronuclear multiple-quantum coherences for better transverse relaxation properties, (ii) concatenation of proton evolution into the simultaneous H-1 and C-13 constant-time period to eliminate separate time periods for proton evolution, and (iii) use of simultaneous H-1 and C-13 constant-time to remove resonance splitting due to multiple two-and three-bond home-and heteronuclear scalar couplings. This general approach for sensitivity enhancement is demonstrated for the HA(CA)(CO)NH triple-resonance experiment. Results on proteins show that, compared with the heteronuclear single-quantum coherence version of the same experiment, on average the sim-CT HMQC version of HA(CA)-(CO)NH exhibits enhancements of similar to 20%.