论文部分内容阅读
A sensitivity enhanced IPAP NMR experiment was described in this paper, which separates the 1 H 15 N doublets into two different spectra to alleviate the problem of resonance overlaps and achieve the accurate measurement of J and residual dipolar coupling constants in proteins. This experiment offered 20%-60% sensitivity enhancement over the original IPAP experiment, and therefore produced more measurable resonances. Pulsed field gradient was used for coherence selection. Water flip back approach was used for water suppression. The sensitivity enhanced IPAP experiment was employed in the measurement of 1 J NH and 1 D NH constants of the protein UBC9.
A sensitivity enhanced IPAP NMR experiment was described in this paper, which separates the 1 H 15 N doublets into two different spectra to alleviate the problem of resonance overlaps and achieve the accurate measurement of J and residual dipolar coupling constants in proteins. This experiment offered 20 % -60% sensitivity enhancement over the original IPAP experiment, and therefore produced more measurable resonances. Pulsed field gradient was used for coherence selection. Water flip back approach was used for water suppression. The sensitivity enhanced IPAP experiment was employed in measurement of 1 J NH and 1 D NH constants of the protein UBC9.