000080365 001__ 80365
000080365 005__ 20180317093603.0
000080365 0247_ $$2doi$$a10.1006/jmre.1998.1381
000080365 037__ $$aARTICLE
000080365 245__ $$aA spectral window in protein NMR revealing cross-relaxation between amide protons
000080365 269__ $$a1998
000080365 260__ $$c1998
000080365 336__ $$aJournal Articles
000080365 520__ $$aThe principle of quenching undesirable indirect external trouble in nuclear Overhauser effect spectroscopy (QUIET-NOESY) relies on a doubly selective inversion of the longitudinal magnetization components of a source spin A and a target spin X to measure the cross-relaxation rate (Overhauser effect) between A and X without significant perturbation by spin diffusion. In 15N-enriched proteins, this can be achieved by using a bilinear rotation decoupling (BIRD) sequence for the selective inversion of amide protons that have a scalar coupling to nitrogen-15. The procedure can be improved by using editing techniques to simplify the resulting NOESY spectra. [on SciFinder (R)]
000080365 700__ $$aMutzenhardt, Pierre
000080365 700__ $$0243177$$aBodenhausen, Geoffrey$$g122795
000080365 773__ $$j132$$k1$$q159-161$$tJournal of Magnetic Resonance
000080365 909CO $$ooai:infoscience.tind.io:80365$$particle$$pSB
000080365 909C0 $$0252152$$pLRMB$$xU10098
000080365 937__ $$aLRMB-ARTICLE-1998-006
000080365 970__ $$a228/LRMB
000080365 973__ $$aEPFL$$rREVIEWED$$sPUBLISHED
000080365 980__ $$aARTICLE