title: 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-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.
mesh_terms: D055598:Chemical Phenomena; D002621:Chemistry; D004815:Epidermal Growth Factor / Q000032:analysis*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D011487:Protein Conformation; D011522:Protons; D012996:Solutions
chemical_list: D011522:Protons; D012996:Solutions; D004815:Epidermal Growth Factor