Abstract
Due to the recent development of NMR spectroscopy, the three-dimensional structures of proteins up to 10 Kd in aqueous solution can be determined in atomic levels. In the present article, we show the intuitive description on the theoretical background of structural determination by NMR, where we take erabutoxin b as an example and compare the structures in aqueous solution and in the crystalline state. Then, we show the three-dimensional structure of mouse epidermal growth factor and human transforming growth factor a determined by NMR. On the basis of the results, we discuss the molecular mechanism of recognition between the epidermal growth factor and its receptor.
