Our research focuses on studying the structure, function and folding of peptides and proteins. The sequence of amino acids in a protein determines its structure and function. How can we deduce these fundamental properties from the sequence? How do proteins fold into their native three dimensional structures which are biologically active? The answers of these questions are the essential elements of structural biology. The methods that are being used in our lab to probe these questions include: (1) A series of simple model peptides that are synthesized chemically or biochemically. (2) Multidimensional NMR measurements. (3) Absorption, CD and fluorescence measurements (4) Computer simulation. We are studying a series of NMDA antagonists, conantokins, which are peptide toxins found in the venom of cone snails. Using the above methods, we are able to determine the structure, function and calcium binding mode of these peptides. We are also studying various structural motifs that designed De novo. The ultimate objective is to design new peptides and proteins with specified functions.