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Sensitivity-enhanced Experiments for the Measurement of J and Dipolar Coupling Constants

✍ Scribed by Dong-Hai Lin; Xin-Li Liao

Publisher
John Wiley and Sons
Year
2010
Tongue
English
Weight
393 KB
Volume
20
Category
Article
ISSN
0256-7660

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✦ Synopsis

Abstract

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.

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