Concepts in Magnetic Resonance Part A (2011). Volume: 38A, Issue: 6. Pages: 280-288. Erik R.P. Zuiderweg, Aikaterini Rousaki et al.
TROSY, Transverse Relaxation Optimized Spectroscopy, was developed more than a decade ago. Since that time, the 15N-1H HSQC-TROSY experiment has become the standard “fingerprint” correlation spectrum for proteins of high molecular weight. In addition, its implementation in protein triple resonance experiments has pushed the boundaries of NMR assignment up to about 100 kDa, making NMR a highly relevant technique in structural biology. TROSY exploits the dipole-CSA cross-correlated relaxation properties of the NH system and selects for the narrowest of the HSQC J-correlation quartet in both dimensions. The original publications and reviews of TROSY use shift operators and/or single transition product operators to describe the TROSY coherence pathways selections. In this review, we offer a familiar Cartesian product operator approach to comprehensively describe all of the events in the modern TROSY pulse sequence such as multiplet selection, gradient coherence selection, gradient quadrature, and sensitivity enhancement.
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Origin and removal of mixed-phase artifacts in gradient sensitivity enhanced heteronuclear single quantum correlation spectra
Origin and removal of mixed-phase artifacts in gradient sensitivity enhanced heteronuclear single quantum correlation spectra
Abstract Here we describe phasing anomalies observed in gradient sensitivity enhanced 15N-1H HSQC spectra, and analyze their origin. It is shown that, as a result of 15N off-resonance effects, dispersive contributions to the 1H signal become detectable, and lead to 15N-offset dependent phase errors. Strategies that effectively suppress these artifacts are presented.
Content Type Journal Article
Category Article
Pages 199-207
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Multiplet-filtered and gradient-selected zero-quantum TROSY experiments for 13C1H3 methyl groups in proteins
Multiplet-filtered and gradient-selected zero-quantum TROSY experiments for 13C1H3 methyl groups in proteins
Abstract Multiplet-filtered and gradient-selected heteronuclear zero-quantum coherence (gsHZQC) TROSY experiments are described for measuring 1Hâ??13C correlations for 13CH3 methyl groups in proteins. These experiments provide improved suppression of undesirable, broad outer components of the heteronuclear zero-quantum multiplet in medium-sized proteins, or in flexible sites of larger proteins, compared to previously described HZQC sequences (Tugarinov et al. in J Am Chem Soc...
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Gradient-enhanced TROSY described with Cartesian product operators
Linear Mode
