Specific 12CβD(2)12CγD(2)S13CεHD(2) isotopomer labeling of methionine to characterize protein dynamics by 1H and 13C NMR relaxation dispersion.

Protein dynamics on the micro- to millisecond time scale is increasingly found to be critical for biological function, as demonstrated by numerous NMR relaxation dispersion studies. Methyl groups are excellent probes of protein interactions and dynamics because of their favorable NMR relaxation properties, which lead to sharp signals in the (1)H and (13)C NMR spectra. Out of the six different methyl-bearing amino acid residue types in proteins, methionine plays a special role because of its extensive side-chain flexibility and the high polarizability of the sulfur atom.

A comprehensive liquid-state heteronuclear and multidimensional NMR study of Laurentian fulvic acid.

The Boreal forest fulvic acid known as Laurentian fulvic acid (LFA) has been interrogated by state of the art heteronuclear and 2D high resolution NMR techniques. It is shown that one can obtain very highly resolved and informative spectra of a traditionally fractionated material. It was possible to observe a proton coupled system of up to seven bonds in the TOCSY spectrum and 329 peaks in the 1H,13C-HSQC spectrum.