Structural characterization of proteins by NMR spectroscopy begins with the process of
sequence specific resonance assignments in which the 1 H, 13 C and 15 N chemical shifts …

Nuclear magnetic resonance (NMR)-based metabolomics relies mostly on 1D NMR;
however, the technique is limited by overlap of the signals from the metabolites. In order to …

Intrinsically disordered proteins (IDPs) or protein regions represent functionally important
biomolecules without unique structure. Their inherent flexibility prevents high-resolution …

Resonance assignment in intrinsically disordered proteins poses a great challenge because
of poor chemical shift dispersion in most of the nuclei that are commonly monitored …

We present a simple approach to rapidly identify amino acid types in proteins from a 2D
spectrum. The method is based on the fact that 13 C β chemical shifts of different amino acid …

A simple triple resonance NMR experiment that leads to the correlation of the backbone
amide resonances of each amino acid residue 'i'with that of residues 'i− 1'and 'i+ 1'in (13 C …

Functional regulation via conformational dynamics is well known in structured proteins but
less well characterized in intrinsically disordered proteins and their complexes. Using NMR …

New 13 C-detected NMR experiments have been devised for molecules in solution and
solid state, which provide chemical shift correlations of methyl groups with high resolution …

While nuclear magnetic resonance (NMR) has had commendable success in atomic-level
investigation of folded proteins, intrinsically unfolded and partially folded proteins have …

This report reviews the progress in the field of NMR relaxation in fluids. The emphasis is on
comparatively simple liquids and solutions of physico-chemical and chemical interest, in …