Proton nuclear magnetic resonance study on the solution conformation of human epidermal growth factor.

This paper describes elucidation of the conformation of the human epidermal growth factor (hEGF) in an aqueous environment, using one- and two-dimensional proton nuclear magnetic resonance methods. The noted structural information obtained is that a rigid core structure is formed by the interplay of the three disulfide bridges and an antiparallel beta-sheet consisting of Val-19 to Glu-24 and Asp-27 to Asn-32. Furthermore, the hydrophobic amino acid residues of the long C-terminal segment fold back to interact locally with residues in the beta-sheet. It is suggested that the C-terminal residues play an inevitable role in the formation of the receptor-binding site.