In three-dimensional and four-dimensional experiments on doubly labelled proteins not only heteronuclear (13C or 15N) but also proton (1H) frequencies are often indirectly monitored, rather than being directly observed. In this communication we show how in these experiments by overlaying 1H and heteronuclear evolutions one can obtain decreased apparent relaxation rates of 1H signals, yielding improved sensitivity. The new method applies to spin pairs like 1H-15N, as in amide groups, or 1H-13C, as in methine groups of alpha or aromatic systems
In this contribution we present a comprehensive approach to study hydrogen bonding in biological and...
NMR studies of protein structures require knowledge of spectral assignments through correlation spec...
The limited chemical shift range of protons and pairwise interaction among all the abundant nuclear ...
In three-dimensional and four-dimensional experiments on doubly labelled proteins not only heteronuc...
NMR spectroscopy is a powerful tool for research on protein dynamics. In the past decade, there has ...
Measuring the nuclear magnetic resonance spectra of low-gamma heteronuclei such as N-15 constitutes ...
Recently, proton-detected magic-angle spinning (MAS) solid-state nuclear magnetic resonance (NMR) sp...
NMR studies of protein structures require knowledge of spectral assignments through correlation spec...
Sequence-specific assignments of the backbone resonances of proteins form the basis for further stud...
Several methods are presented for the selective determination of spin-lattice and spin-spin relaxati...
Values of ’ 5N- ‘H spin-spin coupling constants can be measured in a quantitative manner by recordin...
Relaxation parameters such as longitudinal relaxation are susceptible to artifacts such as spin diff...
Interactions within proteins, with their surrounding, and with other molecules are mediated mostly b...
NMR spin relaxation spectroscopy is a proven method for characterization of the time-scales and ampl...
We describe new correlation experiments suitable for determining long-range 1H–1H distances in 2H,15...
In this contribution we present a comprehensive approach to study hydrogen bonding in biological and...
NMR studies of protein structures require knowledge of spectral assignments through correlation spec...
The limited chemical shift range of protons and pairwise interaction among all the abundant nuclear ...
In three-dimensional and four-dimensional experiments on doubly labelled proteins not only heteronuc...
NMR spectroscopy is a powerful tool for research on protein dynamics. In the past decade, there has ...
Measuring the nuclear magnetic resonance spectra of low-gamma heteronuclei such as N-15 constitutes ...
Recently, proton-detected magic-angle spinning (MAS) solid-state nuclear magnetic resonance (NMR) sp...
NMR studies of protein structures require knowledge of spectral assignments through correlation spec...
Sequence-specific assignments of the backbone resonances of proteins form the basis for further stud...
Several methods are presented for the selective determination of spin-lattice and spin-spin relaxati...
Values of ’ 5N- ‘H spin-spin coupling constants can be measured in a quantitative manner by recordin...
Relaxation parameters such as longitudinal relaxation are susceptible to artifacts such as spin diff...
Interactions within proteins, with their surrounding, and with other molecules are mediated mostly b...
NMR spin relaxation spectroscopy is a proven method for characterization of the time-scales and ampl...
We describe new correlation experiments suitable for determining long-range 1H–1H distances in 2H,15...
In this contribution we present a comprehensive approach to study hydrogen bonding in biological and...
NMR studies of protein structures require knowledge of spectral assignments through correlation spec...
The limited chemical shift range of protons and pairwise interaction among all the abundant nuclear ...