A high resolution 1H NMR study of the solution structure of human epidermal growth factor

J. A. Carver, R. M. Cooke, G. Esposito, I. D. Campbell, H. Gregory, B. Sheard

Research output: Contribution to journalArticlepeer-review


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-αCH spin-spin coupling constants allowed prediction of the secondary structure. Aspects of the tertiary structure are also identified. A pair of antiparallel β-sheets involving residues 18-23 and 28-34 is a dominant feature of the solution structure.

Original languageEnglish (US)
Pages (from-to)77-81
Number of pages5
JournalFEBS Letters
Issue number1
StatePublished - Sep 1 1986


  • (Human EGF)
  • Growth factor
  • NMR
  • Protein structure

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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