Research in the Andersen group focuses on both the fundamental thermodynamics and structural features associated with biorecognition phenomena and practical applications in drug and protein design. The primary biophysical tools employed are spectroscopic: NMR determinations of polypeptide structure and dynamics, IR- and fluorescence-monitored T-jump kinetics for folding pathways, CD studies of the melting of secondary and tertiary structure. Drug design efforts are supported by NMR structural data for protein hormones and enzymes for key steps required for the viability of bacteria. Active programs in mutant protein over-expression, peptide synthesis, and combinatorial synthesis of small molecule inhibitor libraries support this effort. Illustrative projects are briefly outlined in the following paragraphs.