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

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Abstract
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.