Our laboratory specializes in nuclear magnetic resonance (NMR)-based structural biology research. We are particularly interested in understanding the crucial links between the molecular structures, internal dynamics, and biochemical functions of proteins that are of importance to human endeavors. Questions of interest are: What is the connection between a protein's three-dimensional architecture, flexibility of its amino acids and of its structural elements, and its biological function(s)? How do atomic structures and internal dynamics modulate the biochemical activity of proteins? What is the significance of conserved amino acid residues in protein families? Our approach to providing answers to these scientific issues is to use modern multidimensional (2D, 3D, 4D), heteronuclear (1H, 15N, 13C, 2H) solution nuclear magnetic resonance (NMR) spectroscopy in conjunction with complementary biophysical techniques. We are currently investigating the structural and functional properties of several intriguing proteins.