ABSTRACT
Research on NMR spectroscopy has experienced a dramatic explosion during the last decade. This increased interest has been associated in large part with the ap plication of NMR spectroscopy to study the structure of biomolecules, in particu lar peptides and proteins. The development of multidimensional NMR techniques has made it feasible to determine the structure at atomic resolution of polypeptides of up to 30 kDa in solution, and this limit is very likely to increase in the near future. Such development has coincided with an urgent need for methods of struc tural analysis that can help understand the immense variety of biological functions performed by peptides and proteins, since the rapid advancement of modem mol ecular biology is yielding sequence information on polypeptides of biological in terest at an extraordinary pace. NMR spectroscopy is not only a very powerful tool
to elucidate static three-dimensional structures, but also to analyze the conforma tional behavior of flexible peptides and gain insight into their biologically active conformations, to study protein-protein and protein-ligand interactions, and to in vestigate the dynamic properties of polypeptides.
