The research in my group focuses on the structure-function studies of large proteins using multidimensional (2D, 3D, 4D) and multinuclear (1H, 13C, 15N, and possibly 2H) nuclear magnetic resonance (NMR) spectroscopy. We are particularly interested in understanding the relationships between protein structures, internal motions of amino acid residues that comprise these structures, and the proteins' biological functions and regulation. The research requires that the proteins be isotopically enriched with 15N, 13C or 2H for the NMR experiments. My research group has therefore two emphases: one involves protein biochemistry and molecular biology techniques to produce labeled proteins in milligram quantities in prokaryotic or insect cells, a necessary prerequisite for the NMR studies; the other is oriented toward NMR pulse sequence development, NMR-based structure determination, and functional significance of internal motions of atoms within proteins' 3D structures. Several cross-disciplinary NMR-based research projects are currently being conducted in my laboratory.