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Sensitivity‐enhanced Experiments for the Measurement of J and Dipolar Coupling Constants
Author(s) -
Lin DongHai,
Liao XinLi
Publication year - 2002
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.20020200702
Subject(s) - chemistry , sensitivity (control systems) , coupling constant , residual dipolar coupling , dipole , nuclear magnetic resonance , coherence (philosophical gambling strategy) , magnetic dipole–dipole interaction , j coupling , pulsed field gradient , coupling (piping) , analytical chemistry (journal) , resonance (particle physics) , molecular physics , atomic physics , nuclear magnetic resonance spectroscopy , physics , stereochemistry , molecule , materials science , chromatography , quantum mechanics , organic chemistry , electronic engineering , engineering , metallurgy
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.