A high resolution 1H NMR study of the solution structure of human epidermal growth factor

500 MHz 1H NMR studies of human epidermal growth factor are described. The backbone resonances of the 1-48 derivative of hEGF have been assigned using two-dimensional techniques. Analysis of the type and magnitude of the observed sequential nuclear Overhauser effects and the NH-alpha CH spin-spin coupling constants allowed prediction of the secondary structure. Aspects of the tertiary structure are also identified. A pair of antiparallel beta-sheets involving residues 18-23 and 28-34 is a dominant feature of the solution structure.