title: Proton nuclear magnetic resonance study on the solution conformation of human epidermal growth factor.
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.
authors.affiliation: Department of Polymer Science and Engineering, Faculty of Textile Science, Kyoto Institute of Technology, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Makino
authors.forename: M
authors.initials: M
authors.lastname: Morimoto
authors.forename: M
authors.initials: M
authors.lastname: Nishi
authors.forename: S
authors.initials: S
authors.lastname: Sakamoto
authors.forename: A
authors.initials: A
authors.lastname: Tamura
authors.forename: H
authors.initials: H
authors.lastname: Inooka
authors.forename: K
authors.initials: K
authors.lastname: Akasaka
mesh_terms: D001665:Binding Sites; D004815:Epidermal Growth Factor; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D011522:Protons; D011994:Recombinant Proteins; D012996:Solutions; D014867:Water
chemical_list: D011522:Protons; D011994:Recombinant Proteins; D012996:Solutions; D014867:Water; D004815:Epidermal Growth Factor