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

Abstract

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-αCH spin-spin coupling constants allowed prediction of the secondary structure. Aspects of the tertiary structure are also identified. A pair of antiparallel β-sheets involving residues 18–23 and 28–34 is a dominant feature of the solution structure.