Essential processes of life are mediated by enzymes contained within protein complexes and cellular membranes. Several research groups are trying to understand the structural and functional aspects of these critically important molecular assemblies.<br><br>A significant and poorly understood phenomenon is that of protein folding. Researchers are using Raman spectroscopic measurements of the amide bond as well as computational approaches to open up new ways of understanding this highly complex problem. Scientists at Pitt are conducting novel and ground breaking work and are showing how to measure distance changes occurring within enzymes and between proteins in complexes. At the interface of protein biochemistry and organic chemistry, researchers in the department are examining the folding behavior of synthetic, protein-mimetic oligomers.<br><br>Computational work is also exploring a key question of how intermolecular interactions, for example a receptor and its agonist, alter the structure of the molecular assembly. Another important question is how protein structure is altered by its association with a cell membrane. High powered NMR instrumentation is used to study this concept within our department and across campus.