Spatially selective heteronuclear multiple‐quantum coherence (SS HMQC) NMR
spectroscopy is developed for solution studies of proteins. Due to “time‐staggered” …

Recent studies have indicated that the relaxation rate of the 1 H-13 C multiple-quantum
coherence is much slower than that of the 1 H-13 C single-quantum coherence for non …

For methine sites the relaxation rate of 13 C-1 H two-spin coherence is generally slower
than the relaxation rate of the individual 13 C and 1 H single spin coherences. The slower …

Short transverse relaxation times of Cα and Hα single-quantum states in proteins reduce
signal-to-noise ratios of heteronuclear correlation experiments involving transfers of Cα and …

A gradient-and sensitivity-enhanced HMQC experiment has been developed. The sensitivity
of the experiment is increased by factors of2 and 2 over the conventional and gradient …

Scalar couplings observed in nuclear magnetic resonance (NMR) spectra can give
important insights about molecular structures, however they often complicate spectra by …

Protondetected heteronuclear 'H-“N correlation spectroscopy is a useful technique for
facilitating the assignment of proteins with a molecular weight larger than 15 kDa. In these …

A new strategy is demonstrated that simultaneously enhances sensitivity and resolution in
three-or higher-dimensional heteronuclear multiple quantum NMR experiments. The …

Multidimensional nuclear magnetic resonance (NMR) spectroscopy has enabled detailed
characterizations of protein structures and dynamics that are closely linked to functions …

Nuclear magnetic resonance (NMR) spectroscopy is frequently applied in quantitative
chemical analysis (qNMR). It is easy to measure one-dimensional (1D) NMR spectra in a …