The solution structure of the growth factor chimera mEGF/ TGFa44250 has been determined using an extended version of the DYANA procedure for calculating structures from NMR data. The backbone fold and preferred orientation of the domains of the chimera are similar to those found in previous studies of EGF structures, and several H-bonds used as input constraints in those studies were found independently in the chimera. This shows that the modified activity of the chimera does not result from a major structural change. However, the improved precision of the Epidermal growth factor (EGF) [1,2] and transforming growth factor alpha (TGFa).
